A computer model analysis of the active-site coupling mechanism in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
about
The amidase domain of lipoamidase specifically inactivates lipoylated proteins in vivo.2-Oxo acid dehydrogenase multienzyme complexes: domains, dynamics, and design.Structure, expression, and protein engineering of the pyruvate dehydrogenase complex of Escherichia coli.Repeating functional domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.Segmental structure and protein domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Genetic reconstruction in vitro and 1H-n.m.r. spectroscopyInactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species.Mobility in pyruvate dehydrogenase complexes with multiple lipoyl domains.Antibodies against an inter-domain segment of polypeptide chain inhibit active-site coupling in the pyruvate dehydrogenase multienzyme complex
P2860
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P2860
A computer model analysis of the active-site coupling mechanism in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1983
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
A computer model analysis of t ...... e complex of Escherichia coli.
@en
A computer model analysis of t ...... e complex of Escherichia coli.
@nl
type
label
A computer model analysis of t ...... e complex of Escherichia coli.
@en
A computer model analysis of t ...... e complex of Escherichia coli.
@nl
prefLabel
A computer model analysis of t ...... e complex of Escherichia coli.
@en
A computer model analysis of t ...... e complex of Escherichia coli.
@nl
P2093
P2860
P356
P1476
A computer model analysis of t ...... e complex of Escherichia coli.
@en
P2093
P2860
P304
P356
10.1073/PNAS.80.10.2907
P407
P577
1983-05-01T00:00:00Z