Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex
about
Thiamin diphosphate-dependent enzymes: from enzymology to metabolic regulation, drug design and disease modelsSnapshots of Catalysis in the E1 Subunit of the Pyruvate Dehydrogenase Multienzyme ComplexA dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (α-ketoglutarate decarboxylase)At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?Measurement of intrinsic rate constants in the tyrosine hydroxylase reactionPerspective: Defining and quantifying the role of dynamics in enzyme catalysisNuclear magnetic resonance evidence for the role of the flexible regions of the E1 component of the pyruvate dehydrogenase complex from gram-negative bacteria.Experimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observationsConformational ensemble modulates cooperativity in the rate-determining catalytic step in the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex.Reaction mechanisms of thiamin diphosphate enzymes: defining states of ionization and tautomerization of the cofactor at individual steps.Coupled motions in enzyme catalysis.Catalysis in Enzymatic Decarboxylations: Comparison of Selected Cofactor-dependent and Cofactor-independent Examples.Nuclear magnetic resonance approaches in the study of 2-oxo acid dehydrogenase multienzyme complexes--a literature review.Identification of charge transfer transitions related to thiamin-bound intermediates on enzymes provides a plethora of signatures useful in mechanistic studies.Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step.Multiple roles of mobile active center loops in the E1 component of the Escherichia coli pyruvate dehydrogenase complex - Linkage of protein dynamics to catalysis.Bifunctionality of the thiamin diphosphate cofactor: assignment of tautomeric/ionization states of the 4'-aminopyrimidine ring when various intermediates occupy the active sites during the catalysis of yeast pyruvate decarboxylase.Acrylonitrile quenching of trp phosphorescence in proteins: a probe of the internal flexibility of the globular fold.Minimal genome encoding proteins with constrained amino acid repertoire.Conformational dynamics of 1-deoxy-d-xylulose 5-phosphate synthase on ligand binding revealed by H/D exchange MS.Nanoarmoring: strategies for preparation of multi-catalytic enzyme polymer conjugates and enhancement of high temperature biocatalysis.
P2860
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P2860
Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Efficient coupling of catalysi ...... ydrogenase multienzyme complex
@ast
Efficient coupling of catalysi ...... ydrogenase multienzyme complex
@en
Efficient coupling of catalysi ...... ydrogenase multienzyme complex
@nl
type
label
Efficient coupling of catalysi ...... ydrogenase multienzyme complex
@ast
Efficient coupling of catalysi ...... ydrogenase multienzyme complex
@en
Efficient coupling of catalysi ...... ydrogenase multienzyme complex
@nl
prefLabel
Efficient coupling of catalysi ...... ydrogenase multienzyme complex
@ast
Efficient coupling of catalysi ...... ydrogenase multienzyme complex
@en
Efficient coupling of catalysi ...... ydrogenase multienzyme complex
@nl
P2093
P2860
P356
P1476
Efficient coupling of catalysi ...... ydrogenase multienzyme complex
@en
P2093
Frank Jordan
Gary W Brudvig
Gözde Ulas
Jaeyoung Song
Sachin Kale
William Furey
P2860
P304
P356
10.1073/PNAS.0709328105
P407
P577
2008-01-29T00:00:00Z