Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1)

Max J Cryle; James J De Voss

doi:10.1039/b311652b

Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1)

Chem Commun (Camb). 2004 Jan 7:(1):86-7. doi: 10.1039/b311652b. Epub 2003 Nov 17.

Authors

Max J Cryle¹, James J De Voss

Affiliation

¹ Department of Chemistry, University of Queensland, St. Lucia, Brisbane, Australia 4072.

PMID: 14737344
DOI: 10.1039/b311652b

Abstract

Cytochrome p450(BioI)(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.

MeSH terms

Bacillus subtilis / enzymology*
Bacterial Proteins / metabolism*
Carbon / chemistry
Catalysis
Cytochrome P-450 Enzyme System / metabolism*
Escherichia coli / enzymology
Fatty Acids / chemistry
Fatty Acids / metabolism*
Myristic Acid / chemistry
Myristic Acid / metabolism
Pimelic Acids / chemistry
Pimelic Acids / metabolism

Substances

Bacterial Proteins
Fatty Acids
Pimelic Acids
Myristic Acid
Carbon
Cytochrome P-450 Enzyme System
CYP107H1, Bacillus subtilis