Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
about
Evolutionary families of peptidasesElectrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding siteSubstrate-dependent competency of the catalytic triad of prolyl oligopeptidaseInduced-fit mechanism for prolyl endopeptidase.Structure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASEEnzymes and auxiliary factors for GPI lipid anchor biosynthesis and post-translational transfer to proteinsHighly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac diseaseStructural relationship between lipases and peptidases of the prolyl oligopeptidase family.Structural and mechanistic analysis of two prolyl endopeptidases: role of interdomain dynamics in catalysis and specificity.Prolyl oligopeptidase catalysis. Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step.Parasite prolyl oligopeptidases and the challenge of designing chemotherapeuticals for Chagas disease, leishmaniasis and African trypanosomiasisConsumption of gluten with gluten-degrading enzyme by celiac patients: a pilot-study.Immunomodulation of gut-associated lymphoid tissue: current perspectives.Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family.Effects of ionic strength on the catalysis and stability of prolyl oligopeptidaseKinetic Landscape of a Peptide Bond-Forming Prolyl Oligopeptidase.Benzyloxycarbonylprolylprolinal, a transition-state analogue for prolyl oligopeptidase, forms a tetrahedral adduct with catalytic serine, not a reactive cysteine.Kinetic and mechanistic studies of prolyl oligopeptidase from the hyperthermophile Pyrococcus furiosus.Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.
P2860
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P2860
Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
description
1992 nî lūn-bûn
@nan
1992 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
@ast
Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
@en
type
label
Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
@ast
Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
@en
prefLabel
Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
@ast
Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
@en
P2860
P356
P1433
P1476
Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
@en
P2093
P2860
P304
P356
10.1042/BJ2830647
P407
P478
283 ( Pt 3)
P577
1992-05-01T00:00:00Z