Optimizing the Michaelis complex of trimethylamine dehydrogenase: Identification of interactions that perturb the ionization of substrate and facilitate catalysis with trimethylamine base

Journal of Biological Chemistry

Volumn 276, Issue 46, 2001, Pages 42887-42892

  Basran, Jaswir ^a   Sutcliffe, Michael J ^a   Scrutton, Nigel S ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; IONIZATION; ISOTOPES; MUTAGENESIS; POSITIVE IONS; SUBSTRATES;

ELECTRONIC INTERACTIONS;

ENZYMES;

BASE; DEUTERIUM; FLAVINE NUCLEOTIDE; HISTIDINE; NITROGEN; OXIDOREDUCTASE; TRIMETHYLAMINE; TRIMETHYLAMINE DEHYDROGENASE; TYROSINE; UNCLASSIFIED DRUG; CATION; N DEMETHYLASE; RIBOFLAVIN DERIVATIVE;

ALKALINITY; AMINO ACID SEQUENCE; ARTICLE; ATOM; CATALYSIS; COMPLEX FORMATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; IONIZATION; MICHAELIS COMPLEX; MOLECULAR INTERACTION; OXIDATION; PKA; PRIORITY JOURNAL; REACTION ANALYSIS; REDUCTION; SITE DIRECTED MUTAGENESIS; BINDING SITE; CHEMICAL MODEL; CHEMISTRY; ENZYME SPECIFICITY; KINETICS; METABOLISM; PH; PROTEIN BINDING; TEMPERATURE;

BINDING SITES; CATALYSIS; CATIONS; FLAVINS; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, CHEMICAL; OXIDOREDUCTASES, N-DEMETHYLATING; PROTEIN BINDING; SUBSTRATE SPECIFICITY; TEMPERATURE; TYROSINE;

EID: 0035900665     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M108296200     Document Type: Article

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