Structure, mechanism and catalytic duality of thiamine-dependent enzymes

Cellular and Molecular Life Sciences

Volumn 64, Issue 7-8, 2007, Pages 892-905

  Frank, R A W ^a,b   Leeper, F J ^a   Luisi, B F ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b WELLCOME TRUST SANGER INSTITUTE   (United Kingdom)

Author keywords

Allostery; Catalysis; Cooperativity; Enzyme; Molecular evolution; Structure and function; Thiamine diphosphate

Indexed keywords

ACETOLACTATE SYNTHASE; PYRUVATE DECARBOXYLASE; PYRUVATE DEHYDROGENASE; PYRUVATE OXIDASE; PYRUVATE SYNTHASE; THIAMINE; TRANSKETOLASE;

ALLOSTERISM; CATALYSIS; CATALYST; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME STRUCTURE; GENETIC CONSERVATION; MOLECULAR EVOLUTION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION REACTION; PROTEIN RNA BINDING; REVIEW; STRUCTURE ANALYSIS;

ANIMALS; BINDING SITES; CATALYSIS; ENZYMES; EVOLUTION, MOLECULAR; HUMANS; KINETICS; METABOLIC NETWORKS AND PATHWAYS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; THIAMINE PYROPHOSPHATE;

EID: 34247143709     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-007-6423-5     Document Type: Review

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