Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1).
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.
Cryle
Max J
MJ
Department of Chemistry, University of Queensland, St. Lucia, Brisbane, Australia 4072.
De Voss
James J
JJ
D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism*; D002244:Carbon / Q000737:chemistry; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D005227:Fatty Acids / Q000737:chemistry / Q000378:metabolism*; D019814:Myristic Acid / Q000737:chemistry / Q000378:metabolism; D010867:Pimelic Acids / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D005227:Fatty Acids; D010867:Pimelic Acids; D019814:Myristic Acid; D002244:Carbon; D003577:Cytochrome P-450 Enzyme System; C483260:CYP107H1, Bacillus subtilis