PMC:1189074 / 16242-17031
Annnotations
craft-sa-dev
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craft-ca-core-dev
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2_test
{"project":"2_test","denotations":[{"id":"16121256-3054550-86078329","span":{"begin":326,"end":328},"obj":"3054550"},{"id":"16121256-11590124-86078330","span":{"begin":785,"end":787},"obj":"11590124"},{"id":"T51581","span":{"begin":326,"end":328},"obj":"3054550"},{"id":"T54031","span":{"begin":785,"end":787},"obj":"11590124"}],"text":"Successfully targeting Acadm produced a mouse model for MCAD deficiency with features that mimic the clinical, biochemical, and pathologic phenotype found in human patients. MCAD-deficient patients have abnormal plasma and urine metabolites associated with the medium chain–length enzyme specificity. MCAD-deficient patients [15] often display a characteristic urinary hexanoylglycine peak, as was seen in MCAD−/− mice. Acylcarnitine analysis indicated, however, mouse MCAD is more active toward longer chain substrates than the human MCAD enzyme. This finding is similar to that seen with very long-chain acyl-CoA dehydrogenase (VLCAD) where mouse VLCAD is most active toward C16 acyl-substrates as compared to human VLCAD with the most enzymatic activity toward C14 acyl-substrates [16]."}
craft-ca-core-ex-dev
{"project":"craft-ca-core-ex-dev","denotations":[{"id":"T4768","span":{"begin":768,"end":772},"obj":"CHEBI:22221"},{"id":"T4767","span":{"begin":738,"end":747},"obj":"CHEBI_GO_SO_EXT:enzyme"},{"id":"T4766","span":{"begin":718,"end":723},"obj":"GO_PR_EXT:very_long_chain_acyl_CoA_dehydrogenase"},{"id":"T4765","span":{"begin":712,"end":717},"obj":"NCBITaxon:9606"},{"id":"T4764","span":{"begin":681,"end":685},"obj":"CHEBI:22221"},{"id":"T4763","span":{"begin":649,"end":654},"obj":"GO_PR_EXT:very_long_chain_acyl_CoA_dehydrogenase"},{"id":"T4762","span":{"begin":643,"end":648},"obj":"NCBITaxon:10088"},{"id":"T4761","span":{"begin":630,"end":635},"obj":"GO_PR_EXT:very_long_chain_acyl_CoA_dehydrogenase"},{"id":"T4760","span":{"begin":590,"end":628},"obj":"GO_PR_EXT:very_long_chain_acyl_CoA_dehydrogenase"},{"id":"T4759","span":{"begin":590,"end":614},"obj":"CHEBI:61910"},{"id":"T4758","span":{"begin":540,"end":546},"obj":"CHEBI_GO_SO_EXT:enzyme"},{"id":"T4757","span":{"begin":535,"end":539},"obj":"GO_PR_EXT:medium_chain_acyl_CoA_dehydrogenase"},{"id":"T4756","span":{"begin":529,"end":534},"obj":"NCBITaxon:9606"},{"id":"T4755","span":{"begin":469,"end":473},"obj":"GO_PR_EXT:medium_chain_acyl_CoA_dehydrogenase"},{"id":"T4754","span":{"begin":463,"end":468},"obj":"NCBITaxon:10088"},{"id":"T4753","span":{"begin":420,"end":433},"obj":"CHEBI:17387"},{"id":"T4752","span":{"begin":414,"end":418},"obj":"NCBITaxon:10088"},{"id":"T4751","span":{"begin":412,"end":413},"obj":"SO_EXT:sequence_nullness_or_absence"},{"id":"T4750","span":{"begin":410,"end":411},"obj":"SO_EXT:sequence_nullness_or_absence"},{"id":"T4749","span":{"begin":406,"end":410},"obj":"GO_PR_EXT:medium_chain_acyl_CoA_dehydrogenase"},{"id":"T4748","span":{"begin":369,"end":384},"obj":"CHEBI:64390"},{"id":"T4747","span":{"begin":361,"end":368},"obj":"UBERON:0001088"},{"id":"T4746","span":{"begin":301,"end":305},"obj":"GO_PR_EXT:medium_chain_acyl_CoA_dehydrogenase"},{"id":"T4745","span":{"begin":281,"end":287},"obj":"CHEBI_GO_SO_EXT:enzyme"},{"id":"T4744","span":{"begin":229,"end":240},"obj":"CHEBI_EXT:25212"},{"id":"T4743","span":{"begin":223,"end":228},"obj":"UBERON:0001088"},{"id":"T4742","span":{"begin":212,"end":218},"obj":"UBERON:0001969"},{"id":"T4741","span":{"begin":174,"end":178},"obj":"GO_PR_EXT:medium_chain_acyl_CoA_dehydrogenase"},{"id":"T4740","span":{"begin":158,"end":163},"obj":"NCBITaxon:9606"},{"id":"T4739","span":{"begin":111,"end":122},"obj":"CHEBI_EXT:biochemical"},{"id":"T4738","span":{"begin":56,"end":60},"obj":"GO_PR_EXT:medium_chain_acyl_CoA_dehydrogenase"},{"id":"T4737","span":{"begin":40,"end":45},"obj":"NCBITaxon:10088"},{"id":"T4736","span":{"begin":23,"end":28},"obj":"GO_PR_EXT:medium_chain_acyl_CoA_dehydrogenase"}],"text":"Successfully targeting Acadm produced a mouse model for MCAD deficiency with features that mimic the clinical, biochemical, and pathologic phenotype found in human patients. MCAD-deficient patients have abnormal plasma and urine metabolites associated with the medium chain–length enzyme specificity. MCAD-deficient patients [15] often display a characteristic urinary hexanoylglycine peak, as was seen in MCAD−/− mice. Acylcarnitine analysis indicated, however, mouse MCAD is more active toward longer chain substrates than the human MCAD enzyme. This finding is similar to that seen with very long-chain acyl-CoA dehydrogenase (VLCAD) where mouse VLCAD is most active toward C16 acyl-substrates as compared to human VLCAD with the most enzymatic activity toward C14 acyl-substrates [16]."}