FRUCTOSE-6-PHOSPHATE REDUCTASE FROM SALMONELLA GALLINARUM
Author(s) -
Glaci T. Zancan,
Metry Bacila
Publication year - 1964
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.87.3.614-618.1964
Subject(s) - nicotinamide adenine dinucleotide phosphate , biology , fructose , enzyme , nicotinamide , biochemistry , salmonella , dissociation constant , nicotinamide adenine dinucleotide , phosphate , nad+ kinase , bacteria , oxidase test , receptor , genetics
Zancan, Glaci T. (Universidade do Paraná, Curitiba, Paraná, Brazil),and Metry Bacila . Fructose-6-phosphate reductase fromSalmonella gallinarum . J. Bacteriol.87: 614–618. 1964.—A fructose-6-phosphate reductase present in cell-free extracts ofSalmonella gallinarum was purified approximately 42 times. The optimal pH for this enzyme is 8.0. The enzyme is specific for fructose-6-phosphate and reduced nicotinamide adenine dinucleotide (NADH). The dissociation constants are 1.78 × 10−4 m for fructose-6-phosphate and 8.3 × 10−5 m for NADH. The Q10 , reaction order, and equilibrium constant were determined. The enzyme is sensitive top -chloromercuribenzoic acid, but not too -iodosobenzoic acid nor toN -ethylmaleimide.
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