Cytochrome p450 oxygenases
AssigneeCalifornia Institute of Technology
InventorsEdgardo T. Farinas, Frances H. Arnold, Ulrich Schwaneberg, Anton Glieder
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AssigneeCalifornia Institute of Technology
InventorsEdgardo T. Farinas, Frances H. Arnold, Ulrich Schwaneberg, Anton Glieder
Estimating the term…
Nucleic acids encoding cytochrome P450 variants are provided. The cytochrome P450 variants of have a higher alkane-oxidation capability, alkene-oxidation capability, and/or a higher organic-solvent resistance than the corresponding wild-type or parent cytochrome P450 enzyme. A preferred wild-type cytochrome P450 is cytochrome P450 BM-3. Preferred cytochrome P450 variants include those having an improved capability to hydroxylate alkanes and epoxidate alkenes comprising less than 8 carbons, and have amino acid substitutions corresponding to V78A, H236Q, and E252G of cytochrome P450 BM-3. Preferred cytochrome P450 variants also include those having an improved hydroxylation activity in solutions comprising co-solvents such as DMSO and THF, and have amino acid substitutions corresponding to T235A, R471A, E494K, and S1024E of cytochrome P450 BM-3.
1-67. (canceled)
An isolated polypeptide having activity of a cytochrome P450 variant, wherein the variant is characterized as comprising a higher capability than the corresponding wild-type cytochrome P450 to oxidize at least one substrate selected from an alkane comprising a carbon-chain of no more than 8 carbons and an alkene comprising a carbon-chain no more than 8 carbons, and wherein the wild-type cytochrome P450 comprises an amino acid sequence having at least 90% sequence identity to SEQ ID NO:
Dependencies are inferred from the claim text.