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Issue 1, 2004
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Carbon–carbon bond cleavage by cytochrome P450BioI (CYP107H1)

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Abstract

Cytochrome P450BioI (CYP107H1) is believed to supply pimelic acid equivalents for biotin biosynthesis in Bacillus subtilis: we report here that the mechanistic pathway adopted by this multifunctional P450 for the in-chain cleavage of fatty acids is via consecutive formation of alcohol and threo-diol intermediates, with the likely absolute configuration of the intermediates also reported.

Graphical abstract: Carbon–carbon bond cleavage by cytochrome P450BioI (CYP107H1)

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Supplementary files

Article information


Submitted
22 Sep 2003
Accepted
29 Oct 2003
First published
17 Nov 2003

Chem. Commun., 2004, 86-87
Article type
Communication

Carbon–carbon bond cleavage by cytochrome P450BioI (CYP107H1)

M. J. Cryle and J. J. De Voss, Chem. Commun., 2004, 86
DOI: 10.1039/B311652B

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