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EC Tree
IUBMB Comments 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 .
The enzyme appears in viruses and cellular organisms
Synonyms
p450 bioi,
more
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CYP107H1
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fatty acid hydroxylase
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fatty acid hydroxylase
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P450BioI
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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
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
a 7-oxoheptanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O = a pimeloyl-[acyl-carrier protein] + reduced flavodoxin + H+
a long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O2 = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H2O
a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
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
1c
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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
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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
1b
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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
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a 7-oxoheptanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O = a pimeloyl-[acyl-carrier protein] + reduced flavodoxin + H+
1d
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a 7-oxoheptanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O = a pimeloyl-[acyl-carrier protein] + reduced flavodoxin + H+
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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
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a long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O2 = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H2O
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a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
1a
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a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
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acyl-[acyl-carrier protein],reduced-flavodoxin:oxygen oxidoreductase (pimeloyl-[acyl-carrier protein] forming)
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].
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(7R,8R)-7,8-dihydroxytetradecanoyl-[acyl carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + ?
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best substrate
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?
(7R,8S)-7,8-dihydroxytetradecanoyl-[acyl carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + ?
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?
7-hydroxytetradecanoyl-[acyl carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + ?
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?
7-oxotetradecanoyl-[acyl carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + ?
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?
a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + H2O
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r
hexadec-(9Z)-enoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
hexadecanoyl-[acyl-carrier protein] + reduced flavodoxin + O2
11-hydroxyhexadecanoyl-[acyl-carrier protein] + 12-hydroxyhexadecanoyl-[acyl-carrier protein] + 13-hydroxytetradecanoyl-[acyl-carrier protein] + 14-hydroxytetradecanoyl-[acyl-carrier protein] + 15-hydroxytetradecanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
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the enzyme produces mainly the 11- to 15-hydroxy C16 fatty acids
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r
myristoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
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r
octadec-(9Z)-enoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
oleoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
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r
palmitoleoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
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r
palmitoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
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r
tetradecanoyl-[acyl-carrier protein] + reduced flavodoxin + O2
11-hydroxytetradecanoyl-[acyl-carrier protein] + 12-hydroxytetradecanoyl-[acyl-carrier protein] + 14-hydroxytetradecanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
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the enzyme produces mainly the 11-, 12-, and 13-hydroxy C14 fatty acids
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r
tetradecanoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
tetradecanoyl-[acyl-carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl carrier protein] + ?
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r
additional information
?
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hexadec-(9Z)-enoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
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r
hexadec-(9Z)-enoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
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r
octadec-(9Z)-enoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
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r
octadec-(9Z)-enoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
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r
tetradecanoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
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r
tetradecanoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
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r
additional information
?
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CYP107H1 also shows the ortho-specific hydroxylation activity to daidzein, when coupled to the putidaredoxin reductase (camA) and putidaredoxin (camB) from Pseudomonas putida as the redox partners in the presence of NADH and O2 yielding 7,3ā,4_-trihydroxyisoflavone
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additional information
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CYP107H1 also shows the ortho-specific hydroxylation activity to daidzein, when coupled to the putidaredoxin reductase (camA) and putidaredoxin (camB) from Pseudomonas putida as the redox partners in the presence of NADH and O2 yielding 7,3ā,4_-trihydroxyisoflavone
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a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + H2O
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r
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omega-imidazolyl decanoic acid
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omega-imidazolyl lauric acid
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omega-imidazolyl undecanoic acid
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6.9
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calculated from amino acid sequence
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brenda
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brenda
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UniProt
brenda
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metabolism
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the enzyme is involved in biotin biosynthesis
metabolism
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the biosynthetic function of the enzyme is the formation of pimelic acid, a biotin precursor, via a multiple-step oxidative cleavage of long-chain fatty acids
metabolism
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the enzyme plays a putative role in the synthesis of biotin precursor
metabolism
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the enzyme is is involved in biotin biosynthesis
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Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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44705
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x * 44705, estimated from amino acid sequence
45000
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x * 45000, SDS-PAGE
45348
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x * 45348, electrospray ionization mass spectrometry
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?
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x * 45000, SDS-PAGE; x * 45348, electrospray ionization mass spectrometry
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x * 44705, estimated from amino acid sequence
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hanging drop vapor diffusion method, using 0.1 M Na HEPES (pH 6.5), 0.15 M Li2SO4, 0.25 M NaCl, 19% (w/v) PEG 4000, and 0.2% (w/v) n-heptyl beta-D-thioglucopyranoside
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DEAE Sephacel column chromatography, hydroxyapatite column chromatography, Q-Sepharose column chromatography, and Sephacryl S-200 gel filtration
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Ni-NTA affinity column chromatography
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Q-Sepharose column chromatography, DEAE-Sepharose column chromatography, hydroxyapatite column chromatography, and Sephacryl S-300 gel filtration
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli DH5alpha cells
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expressed in Escherichia coli Origami (DE3) cells
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Stok, J.E.; 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
351-360
2000
Bacillus subtilis
brenda
Cryle, M.J.
Selectivity in a barren landscape: the P450BioI-ACP complex
Biochem. Soc. Trans.
38
934-939
2010
Bacillus subtilis
brenda
Lawson, R.J.; Leys, D.; Sutcliffe, M.J.; Kemp, C.A.; Cheesman, M.R.; Smith, S.J.; Clarkson, J.; Smith, W.E.; Haq, I.; Perkins, J.B.; Munro, A.W.
Thermodynamic and biophysical characterization of cytochrome P450 BioI from Bacillus subtilis
Biochemistry
43
12410-12426
2004
Bacillus subtilis
brenda
Cryle, M.J.; De Voss, J.J.
Carbon-carbon bond cleavage by cytochrome p450BioI (CYP107H1)
Chem. Commun. (Camb. )
10
86-87
2004
Bacillus subtilis
brenda
Roh, C.; Choi, K.; Pandey, B.; Kim, B.
Hydroxylation of daidzein by CYP107H1 from Bacillus subtilis 168
J. Mol. Catal. B
59
248-253
2009
Bacillus subtilis, Bacillus subtilis 168
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brenda
Cryle, M.J.; Matovic, N.J.; De Voss, J.J.
Products of cytochrome P450BioI (CYP107H1)-catalyzed oxidation of fatty acids
Org. Lett.
5
3341-3344
2003
Bacillus subtilis
brenda
Cryle, M.J.; Schlichting, I.
Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450BioI ACP complex
Proc. Natl. Acad. Sci. USA
105
15696-15701
2008
Bacillus subtilis (P53554)
brenda
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Transporter Classification Database (TCDB):
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