Information on EC 1.14.13.185 - pikromycin synthase

for references in articles please use BRENDA:EC1.14.13.185
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.185
transferred to EC 1.14.15.33
RECOMMENDED NAME
GeneOntology No.
pikromycin synthase
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of 12-, 14- and 16-membered macrolides
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Biosynthesis of antibiotics
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Q82LM3
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
narbomycin + 2 NADPH + 2 H+ + 2 O2
novapikromyin + 2 NADP+ + 2 H2O
show the reaction diagram
narbomycin + NADPH + H+ + O2
pikromycin + NADP+ + H2O
show the reaction diagram
Q82LM3;
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
narbomycin + 2 NADPH + 2 H+ + 2 O2
novapikromyin + 2 NADP+ + 2 H2O
show the reaction diagram
narbomycin + NADPH + H+ + O2
pikromycin + NADP+ + H2O
show the reaction diagram
Q82LM3
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
Q82LM3;
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heme
Q82LM3;
CYP107L2 shows a low-spin state of heme. Heme is sandwiched between helices I and L in the conserved way of P450 structures. The I-helix crosses the center of CYP107L2 in a slightly bent form over the heme structure, while helices F and G are stacked onto the I-helix to form a wide-open substrate-binding cavity just above the heme moiety
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant ligand-free CYP107L2 and its complex with lauric acid, (1) sitting drop vapor diffusion method, mixing of 500 nl of 12 mg/ml protein solution with 500 nl of reservoir solution containing 0.17 M ammonium sulfate, 0.085 M sodium cacodylate, pH 6.5, 25.5% w/v PEG 8000, and 15% v/v glycerol, for complex crystals lauric acid in a 1:10 M ratio, and equilibration against 0.05 ml of reservoir solution, 14°C, 30 days, (2) hanging drop vapor diffusion method, mixing of 0.001 ml of 12 mg/ml protein solution with 0.001 ml of reservoir solution containing 0.17 M ammonium sulfate, 0.085 M sodium cacodylate, pH 6.5, 25.5% w/v PEG 8000, and 15% v/v glycerol, and equilibration against 0.05 ml of reservoir solution, X-ray diffraction structure determination and analysis at 2.5-2.6 A resolution
Q82LM3;
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Q82LM3;
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene cyp107l2, recombinant expression of His-tagged enzyme in Escherichia coli
Q82LM3;