Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue
about
root uv-b sensitive mutants are suppressed by specific mutations in ASPARTATE AMINOTRANSFERASE2 and by exogenous vitamin B6Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia.Structure modelling and site-directed mutagenesis of the rat aromatic L-amino acid pyridoxal 5'-phosphate-dependent decarboxylase: a functional study.Site-directed mutagenesis provides insight into racemization and transamination of alanine catalyzed by Treponema denticola cystalysin.Identification of disulfide bonds among the nine core 2 N-acetylglucosaminyltransferase-M cysteines conserved in the mucin beta6-N-acetylglucosaminyltransferase family.
P2860
Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Structural basis for the catal ...... osphate-binding lysine residue
@ast
Structural basis for the catal ...... osphate-binding lysine residue
@en
Structural basis for the catal ...... osphate-binding lysine residue
@nl
type
label
Structural basis for the catal ...... osphate-binding lysine residue
@ast
Structural basis for the catal ...... osphate-binding lysine residue
@en
Structural basis for the catal ...... osphate-binding lysine residue
@nl
prefLabel
Structural basis for the catal ...... osphate-binding lysine residue
@ast
Structural basis for the catal ...... osphate-binding lysine residue
@en
Structural basis for the catal ...... osphate-binding lysine residue
@nl
P2093
P356
P1433
P1476
Structural basis for the catal ...... osphate-binding lysine residue
@en
P2093
J N Jansonius
P Christen
V N Malashkevich
P304
P356
10.1021/BI00002A004
P407
P577
1995-01-17T00:00:00Z