The epoxide hydrolase from Rhodotorula glutinis was isolated and initially
characterized. The enzyme was membrane associated and could be solubilized
by Triton X-100. Purification yielded an enzyme with sp. act. of 66 mu mol
1,2-epoxyhexane hydrolyzed min(-1) mg(-1) protein. The enzyme was not compl
etely purified to homogeneity but, nevertheless, a major protein was isolat
ed by SDS-PAGE for subsequential amino acid determination of peptide fragme
nts. From sequence alignments to related enzymes, a high homology towards t
he active site sequences of other microsomal epoxide hydrolases was found.
Molecular mass determinations indicated that the native enzyme exists as a
homodimer, with a subunit molecular mass of about 45 kDa. Based upon these,
this epoxide hydrolase is structurally related to other microsomal epoxide
hydrolases.