Leaving group activation and pyrophosphate ionic state at the catalytic site of Plasmodium falciparum orotate phosphoribosyltransferase.
about
Recycling nicotinamide. The transition-state structure of human nicotinamide phosphoribosyltransferase.Ground state destabilization from a positioned general base in the ketosteroid isomerase active site.Transition state analogues of Plasmodium falciparum and human orotate phosphoribosyltransferases.Ground-state destabilization in orotate phosphoribosyltransferases by binding isotope effects.Isotope-edited FTIR of alkaline phosphatase resolves paradoxical ligand binding properties and suggests a role for ground-state destabilization.
P2860
Leaving group activation and pyrophosphate ionic state at the catalytic site of Plasmodium falciparum orotate phosphoribosyltransferase.
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Leaving group activation and p ...... ate phosphoribosyltransferase.
@ast
Leaving group activation and p ...... ate phosphoribosyltransferase.
@en
Leaving group activation and p ...... ate phosphoribosyltransferase.
@nl
type
label
Leaving group activation and p ...... ate phosphoribosyltransferase.
@ast
Leaving group activation and p ...... ate phosphoribosyltransferase.
@en
Leaving group activation and p ...... ate phosphoribosyltransferase.
@nl
prefLabel
Leaving group activation and p ...... ate phosphoribosyltransferase.
@ast
Leaving group activation and p ...... ate phosphoribosyltransferase.
@en
Leaving group activation and p ...... ate phosphoribosyltransferase.
@nl
P2093
P2860
P356
P1476
Leaving group activation and p ...... ate phosphoribosyltransferase.
@en
P2093
Vern L Schramm
Yong Zhang
P2860
P304
17023-17031
P356
10.1021/JA107806J
P407
P577
2010-11-10T00:00:00Z