Katsushi Nishimura, Teiko Harada, Yasukazu Arita, Hisayuki Watanabe, Hidehiko Iwabuki, Asako Terada, Takafumi Naganuma, Yasuyuki Uzuka
Index: J. Biosci. Bioeng. 101 , 303-308, (2006)
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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.
| Structure | Name/CAS No. | Molecular Formula | Articles |
|---|---|---|---|
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L-(+)-ERYTHROSE
CAS:533-49-3 |
C4H8O4 |
|
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2011-10-01 [J. Microbiol. Biotechnol. 21 , 1064-1068, (2011)] |
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