Benzil was reduced stereospecifically to (S)-benzoin by Bacillus cereus str
ain Tim-r01. To isolate the gene responsible for asymmetric reduction, we c
onstructed a library consisting of Escherichia coli clones that harbored pl
asmids expressing Bacillus cereus genes. The library was screened using the
halo formation assay, and one clone showed benzil reduction to (S)-benzoin
. Thus, this clone seemed to carry a plasmid encoding a Bacillus cereus ben
zil reductase. The deduced amino acid sequence had marked homologies to the
Bacillus subtilis yueD protein (41% identity), the yeast open reading fram
e YIR036C protein (31%), and the mammalian sepiapterin reductases (28% to 3
0%), suggesting that benzil reductase is a novel short-chain de-hydrogenase
s/ reductase. (C) 2001 John Wiley & Sons, Inc.