Rethinking fundamentals of enzyme action.

Rethinking fundamentals of enzyme action.

Item
http://www.wikidata.org/entity/Q33602263
A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from SynechocystisPolyserase-I, a human polyprotease with the ability to generate independent serine protease domains from a single translation product.Phenotype of the most common "slow acetylator" arylamine N-acetyltransferase 1 genetic variant (NAT1*14B) is substrate-dependent.Functional characterization of AlgL, an alginate lyase from Pseudomonas aeruginosaAlternative substrate kinetics of Escherichia coli ribonuclease P: determination of relative rate constants by internal competition.Determination of relative rate constants for in vitro RNA processing reactions by internal competition.Role of non-covalent enzyme-substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda.Phylogenetic sequence analysis and functional studies reveal compensatory amino acid substitutions in loop 2 of human ribonucleotide reductase.
P2860

Rethinking fundamentals of enzyme action.

Item
http://www.wikidata.org/entity/Q33602263
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Rethinking fundamentals of enzyme action.
@ast
Rethinking fundamentals of enzyme action.
@en
type
label
Rethinking fundamentals of enzyme action.
@ast
Rethinking fundamentals of enzyme action.
@en
prefLabel
Rethinking fundamentals of enzyme action.
@ast
Rethinking fundamentals of enzyme action.
@en
P1433
P1476
P2093
P304
P31
P356
P478
P577
P698
P356
P1433
P1476
Rethinking fundamentals of enzyme action
@en
P2093
P304
P31
P356
P478
P577
P698