Steady-state kinetics of cabbage histidinol dehydrogenase.
about
Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase.The role of gene fusions in the evolution of metabolic pathways: the histidine biosynthesis case.Histidine biosynthesis.Depiction of metabolome changes in histidine-starved Escherichia coli by CE-TOFMS.Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD+ Binding and the Cofactor Positioned to Accept a Hydride.Properties and Kinetic Analysis of UDP-glucose Dehydrogenase from Group A Streptococci
P2860
Steady-state kinetics of cabbage histidinol dehydrogenase.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
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1994年學術文章
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name
Steady-state kinetics of cabbage histidinol dehydrogenase.
@en
Steady-state kinetics of cabbage histidinol dehydrogenase.
@nl
type
label
Steady-state kinetics of cabbage histidinol dehydrogenase.
@en
Steady-state kinetics of cabbage histidinol dehydrogenase.
@nl
prefLabel
Steady-state kinetics of cabbage histidinol dehydrogenase.
@en
Steady-state kinetics of cabbage histidinol dehydrogenase.
@nl
P2093
P356
P1476
Steady-state kinetics of cabbage histidinol dehydrogenase.
@en
P2093
P304
P356
10.1006/ABBI.1994.1337
P407
P577
1994-08-01T00:00:00Z