Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy

acyl-[acyl-carrier protein],reduced-flavodoxin:oxygen oxidoreductase (pimeloyl-[acyl-carrier protein] forming)

a long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O2 = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H2O (overall reaction) [RN:R10123];
(1a) a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O;
(1b) a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O;
(1c) a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a 7-oxoheptanoyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + 2 H2O;
(1d) a 7-oxoheptanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O = a pimeloyl-[acyl-carrier protein] + reduced flavodoxin + H+

R10123
Reaction

long-chain acyl-[acyl-carrier protein] [CPD:C20683];
reduced flavodoxin [CPD:C02745];
O2 [CPD:C00007];
(7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein];
(7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein];
7-oxoheptanoyl-[acyl-carrier protein];
oxidized flavodoxin [CPD:C02869];
H2O [CPD:C00001]

A cytochrome P-450 (heme-thiolate) protein. The enzyme catalyses an oxidative C-C bond cleavage of long-chain acyl-[acyl-carrier protein]s of various lengths to generate pimeloyl-[acyl-carrier protein], an intermediate in the biosynthesis of biotin. The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal. The mechanism is similar to EC 1.14.15.6, cholesterol monooxygenase (side-chain-cleaving), followed by a hydroxylation step, which may occur spontaneously [2].

EC 1.14.14.46 created 2013 as EC 1.14.15.12, transferred 2017 to EC 1.14.14.46

1  [PMID:11368323]

Stok JE, De Voss J

Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis.

Arch Biochem Biophys 384:351-60 (2000)
DOI:10.1006/abbi.2000.2067

2  [PMID:14737344]

Cryle MJ, De Voss JJ

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

Chem Commun (Camb) 86-7 (2004)
DOI:10.1039/b311652b

3  [PMID:18838690]

Cryle MJ, Schlichting I

Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.

Proc Natl Acad Sci U S A 105:15696-701 (2008)
DOI:10.1073/pnas.0805983105

[bsu:BSU30190]

4  [PMID:20658980]

Cryle MJ

Selectivity in a barren landscape: the P450(BioI)-ACP complex.

Biochem Soc Trans 38:934-9 (2010)
DOI:10.1042/BST0380934