Properties of Nicotinamide Adenine Dinucleotide Phosphate-Dependent Formate Dehydrogenase from Clostridium thermoaceticum
AUTOR(ES)
Li, Lan-Fun
RESUMO
Li, Lan-Fun (Western Reserve University School of Medicine, Cleveland, Ohio), Lars Ljungdahl, and Harland G. Wood. Properties of nicotinamide adenine dinucleotide phosphate-dependent formate dehydrogenase from Clostridium thermoaceticum. J. Bacteriol. 92: 405–412. 1966.—A nicotinamide adenine dinucleotide phosphate (NADP)-dependent formate dehydrogenase has been isolated from C. thermoaceticum. The enzyme is very sensitive to oxygen and requires sulfhydryl compounds for activity. The apparent Km at 50 C and pH 7.0 for NADP is 5.9 × 10−5m and for formate, 2.2 × 10−4m. The enzyme is most active at about 60 C and at pH values between 7.0 and 9.0. The enzyme catalyzes an exchange between C14O2 and formate, which requires NADP, but net synthesis of formate from CO2 and reduced nicotinamide adenine dinucleotide phosphate could not be demonstrated. The reaction does not involve ferredoxin.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=276256Documentos Relacionados
- Nicotinamide Adenine Dinucleotide Phosphate-Dependent Formate Dehydrogenase from Clostridium thermoaceticum: Purification and Properties
- Effect of glucose starvation on the nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase of yeast.
- Regulation of the Nicotinamide Adenine Dinucleotide- and Nicotinamide Adenine Dinucleotide Phosphate-Dependent Glutamate Dehydrogenases of Saccharomyces cerevisiae
- Regulation of Saccharomyces cerevisiae nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase by proteolysis during carbon starvation.
- Identification of Reduced Nicotinamide Adenine Dinucleotide Phosphate-Dependent Aldehyde Reductase in A Rhodotorula Strain
