BRENDA - Enzyme Database
show all sequences of 1.14.15.33

Structural insights into the binding of lauric acid to CYP107L2 from Streptomyces avermitilis

Han, S.; Pham, T.V.; Kim, J.H.; Lim, Y.R.; Park, H.G.; Jeong, D.; Yun, C.H.; Chun, Y.J.; Kang, L.W.; Kim, D.; Biochem. Biophys. Res. Commun. 482, 902-908 (2017)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene cyp107l2, recombinant expression of His-tagged enzyme in Escherichia coli
Streptomyces avermitilis
Crystallization (Commentary)
Crystallization
Organism
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
Streptomyces avermitilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2
Streptomyces avermitilis
-
novapikromyin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2
Streptomyces avermitilis ATCC 31267
-
novapikromyin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
narbomycin + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Streptomyces avermitilis
-
pikromycin + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
narbomycin + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Streptomyces avermitilis ATCC 31267
-
pikromycin + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces avermitilis
Q82LM3
-
-
Streptomyces avermitilis ATCC 31267
Q82LM3
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Streptomyces avermitilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
no catalytic activity with lauric acid. The lauric acid is bound mainly via hydrophobic interactions with the carboxylate group of lauric acid coordinated to the heme of P450. Residue Glu40 and Leu382 in the CYP107L2 complex with lauric acid show significant conformational changes to provide plentiful room for the lauric acid in the substrate-binding site. Binding structure of enzyme, lauric acid and pikromycin, overview
744239
Streptomyces avermitilis
?
-
-
-
-
additional information
no catalytic activity with lauric acid. The lauric acid is bound mainly via hydrophobic interactions with the carboxylate group of lauric acid coordinated to the heme of P450. Residue Glu40 and Leu382 in the CYP107L2 complex with lauric acid show significant conformational changes to provide plentiful room for the lauric acid in the substrate-binding site. Binding structure of enzyme, lauric acid and pikromycin, overview
744239
Streptomyces avermitilis ATCC 31267
?
-
-
-
-
narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2
-
744239
Streptomyces avermitilis
novapikromyin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2
-
744239
Streptomyces avermitilis ATCC 31267
novapikromyin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
narbomycin + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
-
744239
Streptomyces avermitilis
pikromycin + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
narbomycin + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
-
744239
Streptomyces avermitilis ATCC 31267
pikromycin + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 43000, recombinant His-tagged enzyme, SDS-PAGE and crystal structure analysis
Streptomyces avermitilis
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Streptomyces avermitilis
ferredoxin [iron-sulfur] cluster
-
Streptomyces avermitilis
heme
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
Streptomyces avermitilis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene cyp107l2, recombinant expression of His-tagged enzyme in Escherichia coli
Streptomyces avermitilis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Streptomyces avermitilis
ferredoxin [iron-sulfur] cluster
-
Streptomyces avermitilis
heme
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
Streptomyces avermitilis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
Streptomyces avermitilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2
Streptomyces avermitilis
-
novapikromyin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2
Streptomyces avermitilis ATCC 31267
-
novapikromyin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
narbomycin + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Streptomyces avermitilis
-
pikromycin + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
narbomycin + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
Streptomyces avermitilis ATCC 31267
-
pikromycin + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Streptomyces avermitilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
no catalytic activity with lauric acid. The lauric acid is bound mainly via hydrophobic interactions with the carboxylate group of lauric acid coordinated to the heme of P450. Residue Glu40 and Leu382 in the CYP107L2 complex with lauric acid show significant conformational changes to provide plentiful room for the lauric acid in the substrate-binding site. Binding structure of enzyme, lauric acid and pikromycin, overview
744239
Streptomyces avermitilis
?
-
-
-
-
additional information
no catalytic activity with lauric acid. The lauric acid is bound mainly via hydrophobic interactions with the carboxylate group of lauric acid coordinated to the heme of P450. Residue Glu40 and Leu382 in the CYP107L2 complex with lauric acid show significant conformational changes to provide plentiful room for the lauric acid in the substrate-binding site. Binding structure of enzyme, lauric acid and pikromycin, overview
744239
Streptomyces avermitilis ATCC 31267
?
-
-
-
-
narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2
-
744239
Streptomyces avermitilis
novapikromyin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2
-
744239
Streptomyces avermitilis ATCC 31267
novapikromyin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
narbomycin + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
-
744239
Streptomyces avermitilis
pikromycin + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
narbomycin + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
-
744239
Streptomyces avermitilis ATCC 31267
pikromycin + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 43000, recombinant His-tagged enzyme, SDS-PAGE and crystal structure analysis
Streptomyces avermitilis
General Information
General Information
Commentary
Organism
physiological function
CYP107L1 catalyzes the hydroxylation of narbomycin to produce pikromycin and novapikromycin
Streptomyces avermitilis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
CYP107L1 catalyzes the hydroxylation of narbomycin to produce pikromycin and novapikromycin
Streptomyces avermitilis
Other publictions for EC 1.14.15.33
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744239
Han
Structural insights into the ...
Streptomyces avermitilis, Streptomyces avermitilis ATCC 31267
Biochem. Biophys. Res. Commun.
482
902-908
2017
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1
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727865
Li
Analysis of transient and cata ...
Streptomyces venezuelae
J. Biol. Chem.
284
5723-5730
2009
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1
5
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725370
Sherman
The structural basis for subst ...
Streptomyces venezuelae
J. Biol. Chem.
281
26289-26297
2006
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1
1
3
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6
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1
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6
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12
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1
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1
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728177
Lee
Neopikromycin and novapikromyc ...
Streptomyces venezuelae
J. Nat. Prod.
69
847-849
2006
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714405
Lee
The role of erythromycin C-12 ...
Saccharopolyspora erythraea
Bioorg. Chem.
32
549-559
2004
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1
1
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727289
Xue
Hydroxylation of macrolactones ...
Streptomyces venezuelae
Chem. Biol.
5
661-667
1998
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