Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071.
Two forms of NAD-dependent D-mandelate dehydrogenase (D-ManDHs) were purified from Enterococcus faecalis IAM 10071. While these two enzymes consistently exhibited high activity toward large 2-ketoacid substrates that were branched at the C3 or C4 position, they gave distinctly different K(m) and V(max) values for these substrates and had distinct molecular weights by gel electrophoresis and gel filtration.
Tamura
Yusuke
Y
Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, Noda, Chiba 278-8510, Japan.
Ohkubo
Atsuko
A
Iwai
Saho
S
Wada
Yoichiro
Y
Shinoda
Takeshi
T
Arai
Kazuhito
K
Mineki
Shigeru
S
Iida
Mitsugi
M
Taguchi
Hayao
H
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D013293:Enterococcus faecalis / Q000201:enzymology* / Q000254:growth & development; D007700:Kinetics; D007778:Lactobacillus / Q000201:enzymology; D013294:Lactococcus lactis / Q000201:enzymology; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism*
D009243:NAD; D000429:Alcohol Oxidoreductases; C043630:D-mandelate dehydrogenase