The occurrence of a novel NADH dehydrogenase, distinct from the old yellow enzyme, in Gluconobacter strains.
A novel NADH dehydrogenase (NADH-dh) involving FAD as coenzyme, distinct from NADPH dehydrogenase (NADPH-dh, old yellow enzyme, EC 1.6.99.1), was found in the same cytoplasmic fraction of Gluconobacter strains. Conventional artificial electron acceptors were more effective than molecular oxygen in the NADH-dh reaction. NADH-dh did not appear to be identical with any previously described flavoproteins, although the N-terminal amino acid sequence showed 100% similarity with a non-heme chloroperoxidase. The N-terminal amino acid sequence of NADPH-dh matched 100% a putative oxidoreductase containing the old yellow enzyme-like FMN-binding domain. NADH-dh might function to regenerate NAD coupling with NAD-dependent dehydrogenases in the cytoplasm of Gluconobacter strains.
Shinagawa
Emiko
E
Department of Chemical and Biological Engineering, Ube National College of Technology, Tokiwadai, Ube, Japan. emiko@ube-k.ac.jp
Ano
Yoshitaka
Y
Adachi
Osao
O
Matsushita
Kazunobu
K
D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D005486:Flavin Mononucleotide / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D020576:Gluconobacter / Q000201:enzymology*; D007700:Kinetics; D009245:NADH Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D009252:NADPH Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism
D001426:Bacterial Proteins; D005182:Flavin-Adenine Dinucleotide; D005486:Flavin Mononucleotide; D009252:NADPH Dehydrogenase; D009245:NADH Dehydrogenase