Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase fromhevea brasiliensis

Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase fromhevea brasiliensis

Item
http://www.wikidata.org/entity/Q27620268
The active site of hydroxynitrile lyase from Prunus amygdalus: modeling studies provide new insights into the mechanism of cyanogenesisMechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrinStructure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculentaAtomic resolution crystal structures and quantum chemistry meet to reveal subtleties of hydroxynitrile lyase catalysisSubstrate Binding in the FAD-Dependent Hydroxynitrile Lyase from Almond Provides Insight into the Mechanism of Cyanohydrin Formation and Explains the Absence of Dehydrogenation Activity † , ‡Origin of the Proton-transfer Step in the Cofactor-free (1H)-3-Hydroxy-4-oxoquinaldine 2,4-Dioxygenase: EFFECT OF THE BASICITY OF AN ACTIVE SITE HIS RESIDUEMolecular Basis of the General Base Catalysis of an  / -Hydrolase Catalytic TriadSubstrate specificity of mutants of the hydroxynitrile lyase from Manihot esculenta.Reaction mechanism of hydroxynitrile lyases of the alpha/beta-hydrolase superfamily: the three-dimensional structure of the transient enzyme-substrate complex certifies the crucial role of LYS236.The impact of structural biology on alkaloid biosynthesis research.Elucidation of the mode of substrate binding to hydroxynitrile lyase from Hevea brasiliensis.The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 Å resolution.Observation of a short, strong hydrogen bond in the active site of hydroxynitrile lyase from Hevea brasiliensis explains a large pKa shift of the catalytic base induced by the reaction intermediate.Synergistic computational and experimental proteomics approaches for more accurate detection of active serine hydrolases in yeast.Synthetic 6-aryl-2-hydroxy-6-ketohexa-2,4-dienoic acid substrates for C-C hydrolase BphD: investigation of a general base catalytic mechanism.A QM/MM study of the reaction mechanism of (R)-hydroxynitrile lyases from Arabidopsis thaliana (AtHNL).
P2860

Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase fromhevea brasiliensis

Item
http://www.wikidata.org/entity/Q27620268
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Three-dimensional structures o ...... e lyase fromhevea brasiliensis
@ast
Three-dimensional structures o ...... e lyase fromhevea brasiliensis
@en
Three-dimensional structures o ...... e lyase fromhevea brasiliensis
@nl
type
label
Three-dimensional structures o ...... e lyase fromhevea brasiliensis
@ast
Three-dimensional structures o ...... e lyase fromhevea brasiliensis
@en
Three-dimensional structures o ...... e lyase fromhevea brasiliensis
@nl
prefLabel
Three-dimensional structures o ...... e lyase fromhevea brasiliensis
@ast
Three-dimensional structures o ...... e lyase fromhevea brasiliensis
@en
Three-dimensional structures o ...... e lyase fromhevea brasiliensis
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
Three-dimensional structures o ...... e lyase fromhevea brasiliensis
@en
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932