KEGG   ENZYME: 1.14.14.46
Entry
EC 1.14.14.46               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 flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
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)
R10123
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 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].
History
EC 1.14.14.46 created 2013 as EC 1.14.15.12, transferred 2017 to EC 1.14.14.46
Pathway
ec00780  Biotin metabolism
Orthology
K16593  pimeloyl-[acyl-carrier protein] synthase
Genes
BSU: BSU30190(bioI)
BSR: I33_3073(bioI)
BSL: A7A1_1657
BSH: BSU6051_30190(bioI)
BSY: I653_14450
BSUT: BSUB_03208(bioI)
BSUL: BSUA_03208(bioI)
BSUS: Q433_16375
BSO: BSNT_09439(bioI)
BSN: BSn5_05935
BSQ: B657_30190(bioI)
BSX: C663_2864(bioI)
BSS: BSUW23_14625(bioI)
BST: GYO_3267(bioI)
BLI: BL00957(bioI)
BLD: BLi00771(bioI)
BLH: BaLi_c08690(bioI)
BAQ: BACAU_1782(bioI)
BYA: BANAU_1949(bioI)
BAMP: B938_09435
BAML: BAM5036_1761(bioI)
BAMA: RBAU_1799(bioI)
BAMN: BASU_1779(bioI)
BAMB: BAPNAU_1920(bioI)
BAMT: AJ82_10365
BAMY: V529_17940(bioI)
BMP: NG74_01900(bioI)
BAO: BAMF_1919(bioI)
BAZ: BAMTA208_07910(bioI)
BQL: LL3_02009(bioI)
BXH: BAXH7_01611(bioI)
BQY: MUS_2177(bioI)
BAMI: KSO_010245
BAMC: U471_18790
BAMF: U722_09650
BSON: S101395_00966(bioI)
BACP: SB24_00535
BACB: OY17_12255
BACY: QF06_13285
BACL: BS34A_32830(bioI)
BALM: BsLM_3003
BEO: BEH_11250
BGY: BGLY_0785
BPF: BpOF4_16075(bioI)
BKW: BkAM31D_02760(bioI)
PASA: BAOM_2460(bioI)
ASOC: CB4_02728(bioI)
 » show all
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 384:351-60 (2000)
DOI:10.1006/abbi.2000.2067
Reference
2  [PMID:14737344]
  Authors
Cryle MJ, De Voss JJ
  Title
Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1).
  Journal
Chem Commun (Camb) 86-7 (2004)
DOI:10.1039/b311652b
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 105:15696-701 (2008)
DOI:10.1073/pnas.0805983105
  Sequence
[bsu:BSU30190]
Reference
4  [PMID:20658980]
  Authors
Cryle MJ
  Title
Selectivity in a barren landscape: the P450(BioI)-ACP complex.
  Journal
Biochem Soc Trans 38:934-9 (2010)
DOI:10.1042/BST0380934
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.46
IUBMB Enzyme Nomenclature: 1.14.14.46
ExPASy - ENZYME nomenclature database: 1.14.14.46
BRENDA, the Enzyme Database: 1.14.14.46
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