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.
This journal is © The Royal Society of Chemistry 2012
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Fatty Acids / biosynthesis*
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Fatty Acids / chemistry
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Hydroxylation
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Marinobacter / enzymology
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Mixed Function Oxygenases / genetics
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Mixed Function Oxygenases / metabolism*
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Mutation
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Stereoisomerism
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Substrate Specificity
Substances
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Bacterial Proteins
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Fatty Acids
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Mixed Function Oxygenases