PubMed:10814701 JSON TXT

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CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":352,"end":364},"obj":"Cell"},{"id":"T2","span":{"begin":413,"end":426},"obj":"Cell"},{"id":"T3","span":{"begin":459,"end":475},"obj":"Cell"},{"id":"T4","span":{"begin":523,"end":533},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0001064"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000066"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0001063"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

sentences

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":1156,"end":1160},"obj":"http://purl.obolibrary.org/obo/MAT_0000239"},{"id":"T2","span":{"begin":1510,"end":1514},"obj":"http://purl.obolibrary.org/obo/MAT_0000239"},{"id":"T3","span":{"begin":1702,"end":1706},"obj":"http://purl.obolibrary.org/obo/MAT_0000239"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

PubmedHPO

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":352,"end":358},"obj":"HP_0002664"},{"id":"T2","span":{"begin":523,"end":528},"obj":"HP_0002664"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":28,"end":59},"obj":"http://www.uniprot.org/uniprot/Q06430"},{"id":"T2","span":{"begin":104,"end":135},"obj":"http://www.uniprot.org/uniprot/Q06430"},{"id":"T3","span":{"begin":28,"end":59},"obj":"http://www.uniprot.org/uniprot/Q8N0V5"},{"id":"T4","span":{"begin":104,"end":135},"obj":"http://www.uniprot.org/uniprot/Q8N0V5"},{"id":"T5","span":{"begin":28,"end":59},"obj":"http://www.uniprot.org/uniprot/Q8NFS9"},{"id":"T6","span":{"begin":104,"end":135},"obj":"http://www.uniprot.org/uniprot/Q8NFS9"},{"id":"T7","span":{"begin":142,"end":151},"obj":"http://www.uniprot.org/uniprot/Q09328"},{"id":"T8","span":{"begin":142,"end":151},"obj":"http://www.uniprot.org/uniprot/Q3V5L5"},{"id":"T9","span":{"begin":868,"end":872},"obj":"http://www.uniprot.org/uniprot/P35638"},{"id":"T10","span":{"begin":1361,"end":1364},"obj":"http://www.uniprot.org/uniprot/Q96CY8"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":28,"end":59},"obj":"http://www.uniprot.org/uniprot/P97402"},{"id":"T2","span":{"begin":104,"end":135},"obj":"http://www.uniprot.org/uniprot/P97402"},{"id":"T3","span":{"begin":142,"end":151},"obj":"http://www.uniprot.org/uniprot/Q765H6"},{"id":"T4","span":{"begin":142,"end":151},"obj":"http://www.uniprot.org/uniprot/Q8R4G6"},{"id":"T5","span":{"begin":372,"end":375},"obj":"http://www.uniprot.org/uniprot/P05480"},{"id":"T6","span":{"begin":386,"end":389},"obj":"http://www.uniprot.org/uniprot/P70424"},{"id":"T7","span":{"begin":386,"end":389},"obj":"http://www.uniprot.org/uniprot/O35657"},{"id":"T8","span":{"begin":769,"end":774},"obj":"http://www.uniprot.org/uniprot/O35625"},{"id":"T9","span":{"begin":868,"end":872},"obj":"http://www.uniprot.org/uniprot/P35639"},{"id":"T10","span":{"begin":1361,"end":1364},"obj":"http://www.uniprot.org/uniprot/P28574"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":352,"end":358},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6754"},{"id":"T2","span":{"begin":359,"end":364},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":470,"end":475},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":873,"end":878},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T5","span":{"begin":1361,"end":1364},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1106673"},{"id":"T6","span":{"begin":1754,"end":1759},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/6534"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":28,"end":61},"obj":"http://purl.obolibrary.org/obo/GO_0030144"},{"id":"T2","span":{"begin":104,"end":137},"obj":"http://purl.obolibrary.org/obo/GO_0030144"},{"id":"T3","span":{"begin":305,"end":314},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T4","span":{"begin":399,"end":426},"obj":"http://purl.obolibrary.org/obo/GO_0050863"},{"id":"T5","span":{"begin":399,"end":426},"obj":"http://purl.obolibrary.org/obo/GO_0051132"},{"id":"T6","span":{"begin":399,"end":426},"obj":"http://purl.obolibrary.org/obo/GO_1903905"},{"id":"T7","span":{"begin":399,"end":426},"obj":"http://purl.obolibrary.org/obo/GO_0042110"},{"id":"T8","span":{"begin":399,"end":426},"obj":"http://purl.obolibrary.org/obo/GO_0050798"},{"id":"T9","span":{"begin":873,"end":892},"obj":"http://purl.obolibrary.org/obo/GO_0032940"},{"id":"T10","span":{"begin":884,"end":892},"obj":"http://purl.obolibrary.org/obo/GO_0046903"},{"id":"T11","span":{"begin":980,"end":997},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T12","span":{"begin":1315,"end":1330},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T13","span":{"begin":1082,"end":1100},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T14","span":{"begin":1609,"end":1627},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T15","span":{"begin":1174,"end":1198},"obj":"http://purl.obolibrary.org/obo/GO_0044746"},{"id":"T16","span":{"begin":1174,"end":1198},"obj":"http://purl.obolibrary.org/obo/GO_0044745"},{"id":"T17","span":{"begin":1174,"end":1198},"obj":"http://purl.obolibrary.org/obo/GO_0003333"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":803,"end":814},"obj":"http://purl.obolibrary.org/obo/GO_0019864"},{"id":"T2","span":{"begin":807,"end":814},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":807,"end":814},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T4","span":{"begin":807,"end":814},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T5","span":{"begin":807,"end":814},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":169,"end":174},"obj":"http://purl.obolibrary.org/obo/GO_0005794"},{"id":"T2","span":{"begin":215,"end":219},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T3","span":{"begin":359,"end":364},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":470,"end":475},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":529,"end":533},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":1185,"end":1198},"obj":"http://purl.obolibrary.org/obo/GO_0016021"},{"id":"T7","span":{"begin":1185,"end":1198},"obj":"http://purl.obolibrary.org/obo/GO_0044214"},{"id":"T8","span":{"begin":1226,"end":1235},"obj":"http://purl.obolibrary.org/obo/GO_0005829"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

UBERON-AE

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":1754,"end":1759},"obj":"http://purl.obolibrary.org/obo/UBERON_0002488"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":240,"end":247},"obj":"http://edamontology.org/topic_0602"},{"id":"T2","span":{"begin":352,"end":358},"obj":"http://edamontology.org/topic_2640"},{"id":"T3","span":{"begin":700,"end":708},"obj":"http://edamontology.org/topic_0749"},{"id":"T4","span":{"begin":755,"end":763},"obj":"http://edamontology.org/topic_3168"},{"id":"T5","span":{"begin":755,"end":763},"obj":"http://edamontology.org/topic_0080"},{"id":"T6","span":{"begin":784,"end":792},"obj":"http://edamontology.org/topic_0749"},{"id":"T7","span":{"begin":841,"end":848},"obj":"http://edamontology.org/topic_0078"},{"id":"T8","span":{"begin":841,"end":864},"obj":"http://edamontology.org/topic_0121"},{"id":"T9","span":{"begin":841,"end":864},"obj":"http://edamontology.org/topic_0108"},{"id":"T10","span":{"begin":900,"end":908},"obj":"http://edamontology.org/topic_0078"},{"id":"T11","span":{"begin":1003,"end":1010},"obj":"http://edamontology.org/topic_0154"},{"id":"T12","span":{"begin":1011,"end":1019},"obj":"http://edamontology.org/topic_3168"},{"id":"T13","span":{"begin":1011,"end":1019},"obj":"http://edamontology.org/topic_0080"},{"id":"T14","span":{"begin":1116,"end":1127},"obj":"http://edamontology.org/topic_0154"},{"id":"T15","span":{"begin":1145,"end":1155},"obj":"http://edamontology.org/topic_0154"},{"id":"T16","span":{"begin":1174,"end":1184},"obj":"http://edamontology.org/topic_0154"},{"id":"T17","span":{"begin":1215,"end":1225},"obj":"http://edamontology.org/topic_0154"},{"id":"T18","span":{"begin":1266,"end":1277},"obj":"http://edamontology.org/topic_0154"},{"id":"T19","span":{"begin":1289,"end":1296},"obj":"http://edamontology.org/topic_0154"},{"id":"T20","span":{"begin":1413,"end":1420},"obj":"http://edamontology.org/topic_0154"},{"id":"T21","span":{"begin":1467,"end":1474},"obj":"http://edamontology.org/topic_0154"},{"id":"T22","span":{"begin":1542,"end":1553},"obj":"http://edamontology.org/topic_0154"},{"id":"T23","span":{"begin":1629,"end":1660},"obj":"http://edamontology.org/topic_0178"},{"id":"T24","span":{"begin":1639,"end":1660},"obj":"http://edamontology.org/topic_0082"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":139,"end":141},"obj":"http://edamontology.org/data_1011"},{"id":"T2","span":{"begin":240,"end":247},"obj":"http://edamontology.org/data_2600"},{"id":"T3","span":{"begin":635,"end":641},"obj":"http://edamontology.org/data_2048"},{"id":"T4","span":{"begin":755,"end":763},"obj":"http://edamontology.org/data_2044"},{"id":"T5","span":{"begin":755,"end":763},"obj":"http://edamontology.org/operation_3218"},{"id":"T6","span":{"begin":841,"end":848},"obj":"http://edamontology.org/data_1467"},{"id":"T7","span":{"begin":841,"end":848},"obj":"http://edamontology.org/format_1208"},{"id":"T8","span":{"begin":900,"end":908},"obj":"http://edamontology.org/data_1467"},{"id":"T9","span":{"begin":900,"end":908},"obj":"http://edamontology.org/format_1208"},{"id":"T10","span":{"begin":1003,"end":1010},"obj":"http://edamontology.org/data_2906"},{"id":"T11","span":{"begin":1011,"end":1019},"obj":"http://edamontology.org/data_2044"},{"id":"T12","span":{"begin":1011,"end":1019},"obj":"http://edamontology.org/operation_3218"},{"id":"T13","span":{"begin":1011,"end":1021},"obj":"http://edamontology.org/data_0850"},{"id":"T14","span":{"begin":1289,"end":1296},"obj":"http://edamontology.org/data_2906"},{"id":"T15","span":{"begin":1413,"end":1420},"obj":"http://edamontology.org/data_2906"},{"id":"T16","span":{"begin":1467,"end":1474},"obj":"http://edamontology.org/data_2906"},{"id":"T17","span":{"begin":1629,"end":1660},"obj":"http://edamontology.org/operation_2482"},{"id":"T18","span":{"begin":1629,"end":1660},"obj":"http://edamontology.org/operation_0267"},{"id":"T19","span":{"begin":1629,"end":1660},"obj":"http://edamontology.org/operation_0278"},{"id":"T20","span":{"begin":1639,"end":1648},"obj":"http://edamontology.org/data_0883"},{"id":"T21","span":{"begin":1639,"end":1660},"obj":"http://edamontology.org/operation_2442"},{"id":"T22","span":{"begin":1639,"end":1660},"obj":"http://edamontology.org/operation_2441"},{"id":"T23","span":{"begin":1639,"end":1660},"obj":"http://edamontology.org/operation_0271"},{"id":"T24","span":{"begin":1649,"end":1660},"obj":"http://edamontology.org/operation_2423"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

NGLY1-deficiency

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":67,"end":73},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":153,"end":159},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":283,"end":289},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T4","span":{"begin":446,"end":452},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T5","span":{"begin":563,"end":569},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T6","span":{"begin":722,"end":728},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T7","span":{"begin":745,"end":751},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T8","span":{"begin":1033,"end":1039},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":1156,"end":1160},"obj":"http://purl.obolibrary.org/obo/MAT_0000239"},{"id":"T2","span":{"begin":1510,"end":1514},"obj":"http://purl.obolibrary.org/obo/MAT_0000239"},{"id":"T3","span":{"begin":1702,"end":1706},"obj":"http://purl.obolibrary.org/obo/MAT_0000239"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

performance-test

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1754,"end":1759},"obj":"http://purl.obolibrary.org/obo/UBERON_0002488"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

Lectin

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":372,"end":375},"obj":"https://acgg.asia/db/lfdb/LfDB0103"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

GlyTouCan-IUPAC

mondo_disease

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":352,"end":358},"obj":"Disease"},{"id":"T2","span":{"begin":523,"end":528},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0004992"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":1156,"end":1160},"obj":"Body_part"},{"id":"T2","span":{"begin":1510,"end":1514},"obj":"Body_part"},{"id":"T3","span":{"begin":1702,"end":1706},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000239"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000239"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000239"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":621,"end":625},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10088"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":169,"end":174},"obj":"Body_part"},{"id":"T2","span":{"begin":413,"end":426},"obj":"Body_part"},{"id":"T3","span":{"begin":459,"end":475},"obj":"Body_part"},{"id":"T4","span":{"begin":1185,"end":1198},"obj":"Body_part"},{"id":"T5","span":{"begin":1754,"end":1759},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005794"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000066"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002488"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}

HP-phenotype

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":352,"end":358},"obj":"Phenotype"},{"id":"T2","span":{"begin":523,"end":528},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0002664"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Minimal catalytic domain of N-acetylglucosaminyltransferase V.\nUDP-GlcNAc: Manalpha1-6Manbeta-R beta1-6 N-acetylglucosaminyltransferase V (EC 2.4.1.155, GlcNAc-TV) is a Golgi enzyme that substitutes the trimannosyl core in the biosynthetic pathway for complex-type N-linked glycans. GlcNAc-TV activity is regulated by oncogenes frequently activated in cancer cells ( ras, src, and her2/neu ) and by activators of T lymphocytes. Overexpression of GlcNAc-TV in epithelial cells results in morphological transformation, while tumor cell mutants selected for loss of GlcNAc-TV products show diminished malignant potential in mice. In this report, we have expressed and characterized a series of N- and C-terminal deletions of GlcNAc-TV. Portions of GlcNAc-TV sequence were fused at the N-terminal domain to IgG-binding domains of staphylococcal Protein A and expressed in CHOP cells. The secreted fusion proteins were purified by IgG Sepharose affinity chromatography and assayed for enzyme activities. The peptide sequence S(213-740)of GlcNAc-TV was determined to be essential for the catalytic activity, the remaining amino acids comprising a 183 amino acid stem region, a 17 amino acid transmembrane domain and a 12 amino acid cytosolic moiety. Further deletion of 5 amino acids to produce peptide R(218-740)reduced enzyme activity by 20-fold. Similar K(m)and V(max)values for donor and acceptor were observed for peptide S(213-740), the minimal catalytic domain, and peptide Q(39-740), which also included the stem region. Truncation of five amino acids from the C-terminus also resulted in a 20-fold loss of catalytic activity. Secondary structure predictions suggest a high frequency of turns in the stem region, and more contiguous stretches of alpha-helix found in the catalytic domain."}