Characterization of aldehyde reductase of Sporobolomyces salmonicolor.
An NADPH-dependent aldehyde reductase (EC 1.1.1.2) isolated from Sporobolomyces salmonicolor AKU 4429 was further characterized. The enzyme also catalyzed the reductions of D-glucuronate, D-glucose, D-xylose and D-galactose at high concentrations. Km values for D-glucuronate and D-glucose are 345 and 4270 mM, respectively. Quercetin, dicoumarol and some SH-reagents inhibited the enzyme activity. NH2-terminal amino acid sequence analysis showed that the S. salmonicolor enzyme is partially the same as the aldo-keto reductase family proteins in primary protein structure.
Kataoka
M
M
Department of Agricultural Chemistry, Kyoto University, Japan.
Sakai
H
H
Morikawa
T
T
Katoh
M
M
Miyoshi
T
T
Shimizu
S
S
Yamada
H
H
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D005690:Galactose / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D005965:Glucuronates / Q000378:metabolism; D020723:Glucuronic Acid; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology*; D008969:Molecular Sequence Data; D013379:Substrate Specificity; D014994:Xylose / Q000378:metabolism
D000596:Amino Acids; D005965:Glucuronates; D020723:Glucuronic Acid; D014994:Xylose; D000429:Alcohol Oxidoreductases; C019642:alcohol dehydrogenase (NADP+); D005947:Glucose; D005690:Galactose