title: Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acids.
abstract: CYP153A from Marinobacter aquaeolei has been identified as a fatty acid ω-hydroxylase with a broad substrate range. Two hotspots predicted to influence substrate specificity and selectivity were exchanged. Mutant G307A is 2- to 20-fold more active towards fatty acids than the wild-type. Residue L354 is determinant for the enzyme ω-regioselectivity.
authors.affiliation: Institute of Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany.
authors.forename: Sumire
authors.initials: S
authors.lastname: Honda Malca
authors.forename: Daniel
authors.initials: D
authors.lastname: Scheps
authors.forename: Lisa
authors.initials: L
authors.lastname: Kühnel
authors.forename: Elena
authors.initials: E
authors.lastname: Venegas-Venegas
authors.forename: Alexander
authors.initials: A
authors.lastname: Seifert
authors.forename: Bettina M
authors.initials: BM
authors.lastname: Nestl
authors.forename: Bernhard
authors.initials: B
authors.lastname: Hauer
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D005227:Fatty Acids / Q000096:biosynthesis* / Q000737:chemistry; D006900:Hydroxylation; D053520:Marinobacter / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D005227:Fatty Acids; D006899:Mixed Function Oxygenases