Pyrophosphate activation in hypoxanthine--guanine phosphoribosyltransferase with transition state analogue
about
Leaving group activation and pyrophosphate ionic state at the catalytic site of Plasmodium falciparum orotate phosphoribosyltransferase.The glmS ribozyme tunes the catalytically critical pK(a) of its coenzyme glucosamine-6-phosphateDistortional binding of transition state analogs to human purine nucleoside phosphorylase probed by magic angle spinning solid-state NMR.Enzyme active site interactions by Raman/FTIR, NMR, and ab initio calculationsIsotope-edited FTIR of alkaline phosphatase resolves paradoxical ligand binding properties and suggests a role for ground-state destabilization.
P2860
Pyrophosphate activation in hypoxanthine--guanine phosphoribosyltransferase with transition state analogue
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին 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
Pyrophosphate activation in hy ...... with transition state analogue
@ast
Pyrophosphate activation in hy ...... with transition state analogue
@en
type
label
Pyrophosphate activation in hy ...... with transition state analogue
@ast
Pyrophosphate activation in hy ...... with transition state analogue
@en
prefLabel
Pyrophosphate activation in hy ...... with transition state analogue
@ast
Pyrophosphate activation in hy ...... with transition state analogue
@en
P2093
P2860
P356
P1433
P1476
Pyrophosphate activation in hy ...... with transition state analogue
@en
P2093
Charles Grubmeyer
Robert Callender
Vern L Schramm
P2860
P304
P356
10.1021/BI100012U
P407
P577
2010-03-01T00:00:00Z