Structure-function relationships in human glutathione-dependent formaldehyde dehydrogenase. Role of Glu-67 and Arg-368 in the catalytic mechanism

Biochemistry

Volumn 45, Issue 15, 2006, Pages 4819-4830

  Sanghani, Paresh C ^a   Davis, Wilhelmina I ^b   Zhai, LanMin ^b   Robinson, Howard ^b  

^a INDIANA UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; COMPLEXATION; ISOMERIZATION; ISOTOPES; SUBSTRATES; ZINC;

BINARY COMPLEXES; FORMALDEHYDE DEHYDROGENASE (FDH); KINETIC PATHWAY; STEADY-STATE KINETICS;

ENZYMES;

12 HYDROXYLAURIC ACID; ADENOSINE DIPHOSPHATE RIBOSE; FORMALDEHYDE DEHYDROGENASE; GLUTAMIC ACID; GLUTATHIONE; LAURIC ACID DERIVATIVE; S HYDROXYMETHYLGLUTATHIONE; S NITROSOGLUTATHIONE; UNCLASSIFIED DRUG; ZINC;

ARTICLE; CATALYSIS; DISSOCIATION CONSTANT; ENZYME ACTIVE SITE; ENZYME PURIFICATION; EQUILIBRIUM CONSTANT; ISOMERIZATION; OXIDATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; REDUCTION; SITE DIRECTED MUTAGENESIS; STEADY STATE; STRUCTURE ACTIVITY RELATION; WILD TYPE;

ADENOSINE DIPHOSPHATE RIBOSE; ALDEHYDE OXIDOREDUCTASES; AMINO ACID SUBSTITUTION; ARGININE; CATALYSIS; GLUTAMIC ACID; GLUTATHIONE; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; LAURIC ACIDS; LEUCINE; MODELS, MOLECULAR; PROTEIN CONFORMATION; S-NITROSOGLUTATHIONE; STRUCTURE-ACTIVITY RELATIONSHIP; TIME FACTORS; ZINC;

EID: 33645926683     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052554q     Document Type: Article

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