Structural relationship between lipases and peptidases of the prolyl oligopeptidase family.
about
Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residueElectrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding siteStructure of human carnitine acetyltransferase. Molecular basis for fatty acyl transferReciprocal influence of protein domains in the cold-adapted acyl aminoacyl peptidase from Sporosarcina psychrophila.Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase.Prolyl oligopeptidase catalysis. Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step.OsPOP5, a prolyl oligopeptidase family gene from rice confers abiotic stress tolerance in Escherichia coliEstDZ3: A New Esterolytic Enzyme Exhibiting Remarkable Thermostability.Low molecular weight inhibitors of Prolyl Oligopeptidase: a review of compounds patented from 2003 to 2010.Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family.A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.Aminopeptidase C of Aspergillus niger is a novel phenylalanine aminopeptidaseOverexpression and characterization of a prolyl endopeptidase from the hyperthermophilic archaeon Pyrococcus furiosus.Identification of the active site serine of hormone-sensitive lipase by site-directed mutagenesis.Acylamino acid-releasing enzyme from the thermophilic archaeon Pyrococcus horikoshii.His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate.The purification, characterization and analysis of primary and secondary-structure of prolyl oligopeptidase from human lymphocytes. Evidence that the enzyme belongs to the alpha/beta hydrolase fold family.Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation.
P2860
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P2860
Structural relationship between lipases and peptidases of the prolyl oligopeptidase family.
description
1992 nî lūn-bûn
@nan
1992 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հոտեմբերին 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
Structural relationship betwee ...... prolyl oligopeptidase family.
@ast
Structural relationship betwee ...... prolyl oligopeptidase family.
@en
type
label
Structural relationship betwee ...... prolyl oligopeptidase family.
@ast
Structural relationship betwee ...... prolyl oligopeptidase family.
@en
prefLabel
Structural relationship betwee ...... prolyl oligopeptidase family.
@ast
Structural relationship betwee ...... prolyl oligopeptidase family.
@en
P2860
P1433
P1476
Structural relationship betwee ...... prolyl oligopeptidase family.
@en
P2093
P2860
P304
P356
10.1016/0014-5793(92)81120-B
P407
P577
1992-10-01T00:00:00Z