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Substrate specificity of native and mutated cytochrome P450 (CYP102A3) from Bacillus subtilis
Oliver Lentz1, Vlada Urlacher, Rolf D Schmid
1Institut für Technische Biochemie, Universität Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany.
Abstract:
Within the Bacillus subtilis genome sequencing project, two monooxygenases (CYP102A2 and CYP102A3) were discovered which revealed a similarity of 76% to the well-known cytochrome P450 BM-3 (CYP102A1) of Bacillus megaterium. All enzymes are natural fusion proteins consisting of a heme domain and a reductase domain. We here report the cloning, expression and characterization of B. subtilis enzyme CYP102A3. The substrate specificity of this enzyme is similar to that of B. megaterium CYP102A1, which hydroxylates medium-chain fatty acids in subterminal positions. A double mutant was prepared that hydroxylates a number of other substrates, which do not bear any resemblance to the natural substrate of this enzyme family.
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