Cofactor activation and substrate binding in pyruvate decarboxylase. Insights into the reaction mechanism from molecular dynamics simulations

Biochemistry

Volumn 44, Issue 45, 2005, Pages 14792-14806

  Lie, Mette Alstrup ^a   Celik, Leyla ^b   Jørgensen, Karl Anker ^a   Schiøtt, Birgit ^b  

^a DANISH NATIONAL RESEARCH FOUNDATION   (Denmark)

^b AARHUS UNIVERSITY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTAL STRUCTURE; HYDROGEN BONDS; MOLECULAR DYNAMICS; PROTONS;

PYRUVATE; PYRUVATE DECARBOXYLASE; ZYMOMONAS MOBILIS;

ENZYME KINETICS;

1',4' IMINOPYRIMIDINE THIAMINE DIPHOSPHATE; 4' AMINOPYRIDINE THIAMINE DIPHOSPHATE; 4' AMINOPYRIDINIUM THIAMINE DIPHOSPHATE; ALANINE; ASPARTIC ACID; BACTERIAL ENZYME; BIOLOGICAL FACTOR; CARBONYL DERIVATIVE; COCARBOXYLASE; COFACTOR; GLUTAMIC ACID; HISTIDINE; OXYGEN; PYRUVATE DECARBOXYLASE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; DEPROTONATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GEOMETRY; HYDROGEN BOND; ISOMER; MOLECULAR DYNAMICS; MOLECULAR MODEL; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; REACTION ANALYSIS; SIMULATION; TAUTOMER; ZYMOMONAS MOBILIS;

BINDING SITES; CATALYTIC DOMAIN; COMPUTER SIMULATION; HYDROGEN BONDING; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTATION; PYRUVATE DECARBOXYLASE; PYRUVIC ACID; THIAMINE PYROPHOSPHATE; ZYMOMONAS;

BACTERIA (MICROORGANISMS); ZYMOMONAS MOBILIS;

EID: 27744460562     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051134y     Document Type: Article

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