Dimers generated from tetrameric phosphorylating glyceraldehyde-3- phosphate dehydrogenase from Bacillus stearothermophilus are inactive but exhibit cooperativity in NAD binding

Biochemistry

Volumn 38, Issue 49, 1999, Pages 16084-16091

  Roitel, Olivier ^a   Sergienko, Eduard ^a,b   Branlant, Guy ^a  

^a Biopôle de l Université de Lorraine   (France)

^b The State University of New Jersey   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DIMER; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; TETRAMER;

ARTICLE; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; GEOBACILLUS STEAROTHERMOPHILUS; HYDROGEN BOND; MOLECULAR MODEL; MOLECULAR WEIGHT; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; BACILLUS STEAROTHERMOPHILUS; BINDING SITES; CENTRIFUGATION, DENSITY GRADIENT; DIMERIZATION; ENZYME ACTIVATION; ESCHERICHIA COLI; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NAD; PHOSPHORYLATION; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY;

EID: 0033534147     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9912802     Document Type: Article

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