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Enzyme Nomenclature
Information on EC 1.14.15.12 - pimeloyl-[acyl-carrier protein] synthase
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The expected taxonomic range for this enzyme is: Bacillus subtilis
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EC NUMBER 
COMMENTARY 
1.14.15.12
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RECOMMENDED NAME
GeneOntology No.
pimeloyl-[acyl-carrier protein] synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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-
-
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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
-
-
-
-
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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein],reduced-flavodoxin:oxygen oxidoreductase (pimeloyl-[acyl-carrier protein] forming)
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].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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
-
the enzyme plays a putative role in the synthesis of biotin precursor
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7R,8R)-7,8-dihydroxytetradecanoyl-[acyl carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + ?
-
best substrate
-
-
?
(7R,8S)-7,8-dihydroxytetradecanoyl-[acyl carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + ?
-
-
-
-
?
7-hydroxytetradecanoyl-[acyl carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + ?
-
-
-
-
?
7-oxotetradecanoyl-[acyl carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + ?
-
-
-
-
?
a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + H2O
-
-
-
-
r
hexadecanoyl-[acyl-carrier protein] + reduced flavodoxin + O2
11-hydroxyhexadecanoyl--[acyl-carrier protein] + 12-hydroxyhexadecanoyl-[acyl-carrier protein] + 13-hydroxytetradecanoxl-[acyl-carrier protein] + 14-hydroxytetradecanoxl-[acyl-carrier protein] + 15-hydroxytetradecanoxl-[acyl-carrier protein] + oxidized flavodoxin + H2O
-
-
the enzyme produces mainly the 11- to 15-hydroxy C16 fatty acids
-
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
-
r
tetradecanoyl-[acyl-carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl carrier protein] + ?
-
-
-
-
r
hexadec-(9Z)-enoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
-
-
-
-
r
hexadec-(9Z)-enoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
-
-
-
r
octadec-(9Z)-enoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
-
-
-
-
r
octadec-(9Z)-enoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
-
-
-
r
tetradecanoyl-[acyl-carrier protein] + reduced flavodoxin + O2
?
-
-
-
r
additional information
?
-
-
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 7,3,4_-trihydroxyisoflavone
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-
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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 7,3,4_-trihydroxyisoflavone
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2
pimeloyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + H2O
-
-
-
-
r
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 45000, SDS-PAGE; x * 45348, electrospray ionization mass spectrometry
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE Sephacel column chromatography, hydroxyapatite column chromatography, Q-Sepharose column chromatography, and Sephacryl S-200 gel filtration
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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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.15.12)
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