Identification of enzyme responsible for erythritol utilization and reaction product in yeast Lipomyces starkeyi.
We have identified the enzyme responsible for erythritol utilization and its reaction product in the yeast Lipomyces starkeyi CBS 1807. The enzyme, a polyol dehydrogenase requiring NAD+ as a coenzyme, was induced by erythritol in this yeast. We confirmed that the enzyme product was L-erythrulose by MS, NMR, and polarimeter analyses, meaning that we clarified the first step of erythritol utilization in yeasts for the first time. In the case of the oxidative reaction, D-threitol, (2R,3R)-2,3-butanediol, and erythritol were much better substrates than 21 other polyols tested. These three substrates are tetroses and have an R configuration at C-3, and whose third carbon results in easiest oxidation in this enzyme. The research of the substrate specificity in the reductive reaction demonstrated that L-erythrulose and dihydroxyacetone were better substrates, that D-acetoin was inactive and L-erythrose (aldose) was slightly active.
Nishimura
Katsushi
K
Department of Materials and Applied Chemistry, College of Science and Technology, Nihon University, 1-8-14 Kanda-surugadai, Chiyoda-ku, Tokyo 101-8308, Japan. nisimura@chem.cst.nihon-u.ac.jp
Harada
Teiko
T
Arita
Yasukazu
Y
Watanabe
Hisayuki
H
Iwabuki
Hidehiko
H
Terada
Asako
A
Naganuma
Takafumi
T
Uzuka
Yasuyuki
Y
D001203:Ascomycota / Q000201:enzymology* / Q000378:metabolism*; D001709:Biotechnology / Q000379:methods; D002241:Carbohydrates / Q000737:chemistry; D002474:Cell-Free System; D004098:Dihydroxyacetone / Q000737:chemistry; D004896:Erythritol / Q000378:metabolism*; D007064:L-Iditol 2-Dehydrogenase / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D020539:Sequence Analysis, Protein; D013379:Substrate Specificity
D002241:Carbohydrates; D007064:L-Iditol 2-Dehydrogenase; D004098:Dihydroxyacetone; D004896:Erythritol