KEGG   ENZYME: 1.14.15.12Help
Entry
EC 1.14.15.12               Enzyme                                 

Name
pimeloyl-[acyl-carrier protein] synthase;
bioI (gene name);
P450BioI;
CYP107H1
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
acyl-[acyl-carrier protein],reduced-flavodoxin:oxygen oxidoreductase (pimeloyl-[acyl-carrier protein] forming)
Reaction(IUBMB)
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+
Reaction(KEGG)
Substrate
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]
Product
pimeloyl-[acyl-carrier protein] [CPD:C19845];
n-alkanal [CPD:C15596];
oxidized flavodoxin [CPD:C02869];
H2O [CPD:C00001];
(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];
reduced flavodoxin [CPD:C02745];
H+ [CPD:C00080]
Comment
A heme-thiolate protein (P-450). 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].
History
EC 1.14.15.12 created 2013
Pathway
Biotin metabolism
Orthology
K16593  
pimeloyl-[acyl-carrier protein] synthase
Genes
GSN: 
BSU: 
BSU30190(bioI)
BSR: 
I33_3073(bioI)
BSL: 
BSH: 
BSY: 
BSUT: 
BSUL: 
BSUS: 
BSS: 
BST: 
GYO_3267(bioI)
BSO: 
BSN: 
BSQ: 
BSX: 
C663_2864(bioI)
BSP: 
BLI: 
BL00957(bioI)
BLD: 
BLi00771(bioI)
BLH: 
BAY: 
BAQ: 
BYA: 
BAMP: 
BAML: 
BAMA: 
RBAU_1799(bioI)
BAMN: 
BASU_1779(bioI)
BAMB: 
BAMT: 
BAMY: 
BMP: 
BAO: 
BAMF_1919(bioI)
BAZ: 
BQL: 
LL3_02009(bioI)
BXH: 
BQY: 
MUS_2177(bioI)
BAMI: 
BAMC: 
BAMF: 
BAE: 
BATR: 
BPF: 
BACP: 
BACB: 
BACY: 
BACL: 
BALM: 
BEO: 
 » show all
Taxonomy
Reference
1  [PMID:11368323]
  Authors
Stok JE, De Voss J.
  Title
Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis.
  Journal
Arch. Biochem. Biophys. 384 (2000) 351-60.
  Sequence
[bsu:BSU30190]
Reference
2  [PMID:14737344]
  Authors
Cryle MJ, De Voss JJ
  Title
Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1).
  Journal
Chem. Commun. (Camb).  (2004) 86-7.
  Sequence
[bsu:BSU30190]
Reference
3  [PMID:18838690]
  Authors
Cryle MJ, Schlichting I.
  Title
Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 15696-701.
  Sequence
[bsu:BSU30190]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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