We cloned and characterized the epoxide hydrolase gene, EPH1, from Rhodotor
ula glutinis. The EPH1 open reading frame of 1230 bp was interrupted by nin
e introns and encoded a polypeptide of 409 amino acids with a calculated mo
lecular mass of 46.3 kDa. The amino acid sequence was similar to that of mi
crosomal epoxide hydrolase, which suggests that the epoxide hydrolase of R.
glutinis also belongs to the alp hydrolase fold family. EPH1 cDNA was expr
essed in Escherichia coli and resting cells showed a specific activity of 2
00 nmol min(-1) (mg protein)(-1) towards 1,2-epoxyhexane.