Maeda M, Hosomi S, Mizoguchi T, Nishihara T
Faculty of Pharmaceutical Sciences, Osaka University, Yamada-oka, Suita, Osaka 565-0871.
J Biochem. 1998 Apr;123(4):602-6. doi: 10.1093/oxfordjournals.jbchem.a021979.
We have discovered new characteristics of D-erythrulose reductase, namely, that it can catalyze reduction of not only D-erythrulose but also such diketones as diacetyl. These substrates have a common structure with two neighboring carbonyls possibly in s-cis plane structure, showing that the enzyme may rigorously distinguish between substrates and other compounds. D-Erythrulose reductase was predominantly located in the kidney and the liver of the chicken. The obtained results suggest that D-erythrulose reductase plays an important role in metabolizing alpha-dicarbonyls in animal organs, because these diketones widely occur in natural foods.