pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15).
about
The role of Tyr605 and Ala607 of thimet oligopeptidase and Tyr606 and Gly608 of neurolysin in substrate hydrolysis and inhibitor bindingThe cysteine-rich protein thimet oligopeptidase as a model of the structural requirements for S-glutathiolation and oxidative oligomerization.Hydrogen bond residue positioning in the 599-611 loop of thimet oligopeptidase is required for substrate selectionCleavage site analysis of a serralysin-like protease, PrtA, from an insect pathogen Photorhabdus luminescens and development of a highly sensitive and specific substrate.Flexibility in substrate recognition by thimet oligopeptidase as revealed by denaturation studies.
P2860
pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15).
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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name
pH dependence studies provide ...... oligopeptidase (EC 3.4.24.15).
@en
pH dependence studies provide ...... anism of thimet oligopeptidase
@nl
type
label
pH dependence studies provide ...... oligopeptidase (EC 3.4.24.15).
@en
pH dependence studies provide ...... anism of thimet oligopeptidase
@nl
prefLabel
pH dependence studies provide ...... oligopeptidase (EC 3.4.24.15).
@en
pH dependence studies provide ...... anism of thimet oligopeptidase
@nl
P2093
P2860
P1433
P1476
pH dependence studies provide ...... oligopeptidase (EC 3.4.24.15).
@en
P2093
Amanda Pabon
Jeffrey A Sigman
Marc J Glucksman
Sarah R Edwards
P2860
P304
P356
10.1016/S0014-5793(03)00548-9
P407
P577
2003-06-01T00:00:00Z