Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-139 |
Sentence |
denotes |
Mutational studies on endo-beta-N-acetylglucosaminidase D which hydrolyzes core portion of asparagine-linked complex type oligosaccharides. |
TextSentencer_T2 |
140-371 |
Sentence |
denotes |
Endo-beta-N-acetylglucosaminidase D (Endo D) produced by Streptococcus pneumoniae hydrolyzes the di-N-acetylchitobiose structure in the core of complex-type asparagine-linked oligosaccharides, and has a molecular weight of 180 kDa. |
TextSentencer_T3 |
372-521 |
Sentence |
denotes |
A truncated Endo D of 102 kDa in which 134 N-terminal amino acids and 599 C-terminal amino acids were deleted, still retained the enzymatic activity. |
TextSentencer_T4 |
522-699 |
Sentence |
denotes |
The truncated Endo D has specificity indistinguishable from the intact enzyme, and also acted on the core structure of asparagine-linked oligosaccharides attached to intact IgG. |
TextSentencer_T5 |
700-812 |
Sentence |
denotes |
Because of its lower molecular weight, the truncated enzyme may be useful as a tool for protein deglycosylation. |
TextSentencer_T6 |
813-1008 |
Sentence |
denotes |
The entire region of the truncated Endo D had 32% sequence identity to endo- beta-N-acetylglucosaminidase BH (Endo BH) from Bacillus halodurans, which acted on high-mannose type oligosaccharides. |
TextSentencer_T7 |
1009-1084 |
Sentence |
denotes |
Chimeric constructs of the truncated Endo D and Endo BH showed no activity. |
TextSentencer_T8 |
1085-1198 |
Sentence |
denotes |
Glutamic acid 324 (E 324) in Endo D is conserved in Endo BH and Endo M, and is an essential amino acid in Endo M. |
TextSentencer_T9 |
1199-1242 |
Sentence |
denotes |
Mutation of E324 abolished Endo D activity. |
TextSentencer_T10 |
1243-1367 |
Sentence |
denotes |
The specificity of Endo D for complex type oligosaccharides is probably defined by multiple domains in the Endo D structure. |
T1 |
0-139 |
Sentence |
denotes |
Mutational studies on endo-beta-N-acetylglucosaminidase D which hydrolyzes core portion of asparagine-linked complex type oligosaccharides. |
T2 |
140-371 |
Sentence |
denotes |
Endo-beta-N-acetylglucosaminidase D (Endo D) produced by Streptococcus pneumoniae hydrolyzes the di-N-acetylchitobiose structure in the core of complex-type asparagine-linked oligosaccharides, and has a molecular weight of 180 kDa. |
T3 |
372-521 |
Sentence |
denotes |
A truncated Endo D of 102 kDa in which 134 N-terminal amino acids and 599 C-terminal amino acids were deleted, still retained the enzymatic activity. |
T4 |
522-699 |
Sentence |
denotes |
The truncated Endo D has specificity indistinguishable from the intact enzyme, and also acted on the core structure of asparagine-linked oligosaccharides attached to intact IgG. |
T5 |
700-812 |
Sentence |
denotes |
Because of its lower molecular weight, the truncated enzyme may be useful as a tool for protein deglycosylation. |
T6 |
813-1008 |
Sentence |
denotes |
The entire region of the truncated Endo D had 32% sequence identity to endo- beta-N-acetylglucosaminidase BH (Endo BH) from Bacillus halodurans, which acted on high-mannose type oligosaccharides. |
T7 |
1009-1084 |
Sentence |
denotes |
Chimeric constructs of the truncated Endo D and Endo BH showed no activity. |
T8 |
1085-1198 |
Sentence |
denotes |
Glutamic acid 324 (E 324) in Endo D is conserved in Endo BH and Endo M, and is an essential amino acid in Endo M. |
T9 |
1199-1242 |
Sentence |
denotes |
Mutation of E324 abolished Endo D activity. |
T10 |
1243-1367 |
Sentence |
denotes |
The specificity of Endo D for complex type oligosaccharides is probably defined by multiple domains in the Endo D structure. |