Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.

Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.

Item
http://www.wikidata.org/entity/Q43560031
Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylaseStructural and functional basis for (S)-allantoin formation in the ureide pathwayStructural Characterization of the Molecular Events during a Slow Substrate–Product Transition in Orotidine 5′-Monophosphate DecarboxylaseMechanism of the Orotidine 5′-Monophosphate Decarboxylase-Catalyzed Reaction: Evidence for Substrate Destabilization ,Conformational Changes in Orotidine 5′-Monophosphate Decarboxylase: A Structure-Based Explanation for How the 5′-Phosphate Group Activates the EnzymeSubstrate Distortion Contributes to the Catalysis of Orotidine 5′-Monophosphate DecarboxylaseProton transfer from C-6 of uridine 5'-monophosphate catalyzed by orotidine 5'-monophosphate decarboxylase: formation and stability of a vinyl carbanion intermediate and the effect of a 5-fluoro substituentMechanism of OMP decarboxylation in orotidine 5'-monophosphate decarboxylase.Determination of the amino acid sequence requirements for catalysis by the highly proficient orotidine monophosphate decarboxylase.Molecular dynamic study of orotidine-5'-monophosphate decarboxylase in ground state and in intermediate state: a role of the 203-218 loop dynamics.Investigating the role of a backbone to substrate hydrogen bond in OMP decarboxylase using a site-specific amide to ester substitution.Antifungal effect and mechanism of garlic oil on Penicillium funiculosum.Characterizing selective pressures on the pathway for de novo biosynthesis of pyrimidines in yeastUsing catalytic atom maps to predict the catalytic functions present in enzyme active sites.Indiscriminate binding by orotidine 5'-phosphate decarboxylase of uridine 5'-phosphate derivatives with bulky anionic c6 substituents.Dissecting the total transition state stabilization provided by amino acid side chains at orotidine 5'-monophosphate decarboxylase: a two-part substrate approach.Orotic acid decarboxylation in water and nonpolar solvents: a potential role for desolvation in the action of OMP decarboxylase.
P2860

Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.

Item
http://www.wikidata.org/entity/Q43560031
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.
@en
Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.
@nl
type
label
Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.
@en
Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.
@nl
prefLabel
Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.
@en
Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698