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show all sequences of 1.14.13.217

Expression, crystallization and preliminary crystallographic data analysis of VioD, a hydroxylase in the violacein-biosynthesis pathway

Ran, T.; Gao, M.; Wei, Q.; He, J.; Tang, L.; Wang, W.; Xu, D.; Acta crystallogr. Sect. F 71, 149-152 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene vioD, recombinant expression of His-tagged enzyme in Escherichia coli
Chromobacterium violaceum
Crystallization (Commentary)
Crystallization
Organism
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 7.5-15 mg/ml protein in 20 mM Tris–HCl pH 8.0, 300 mM NaCl, 10% glycerol, with 0.001 ml of reservoir solution containing 3.5 M sodium formate pH 7.0, and equilibration against 0.05 ml of reservoir solution, 2 weeks, X-ray diffraction structure determination and analysis at 1.7 A resolution, solvent-content calculation and molecular-replacement results suggest the presence of two molecules of VioD in the asymmetric unit
Chromobacterium violaceum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Chromobacterium violaceum
enzyme VioD is a flavin-dependent oxygenase that catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein
?
-
-
-
protodeoxyviolaceinate + NAD(P)H + H+ + O2
Chromobacterium violaceum
-
protoviolaceinate + NAD(P)+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chromobacterium violaceum
A0A024AX32
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, ultrafiltration, and gel filtration
Chromobacterium violaceum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
enzyme VioD is a flavin-dependent oxygenase that catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein
735402
Chromobacterium violaceum
?
-
-
-
-
protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
735402
Chromobacterium violaceum
protoviolaceinate + NAD(P)+
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Chromobacterium violaceum
NADPH
-
Chromobacterium violaceum
Cloned(Commentary) (protein specific)
Commentary
Organism
gene vioD, recombinant expression of His-tagged enzyme in Escherichia coli
Chromobacterium violaceum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Chromobacterium violaceum
NADPH
-
Chromobacterium violaceum
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 7.5-15 mg/ml protein in 20 mM Tris–HCl pH 8.0, 300 mM NaCl, 10% glycerol, with 0.001 ml of reservoir solution containing 3.5 M sodium formate pH 7.0, and equilibration against 0.05 ml of reservoir solution, 2 weeks, X-ray diffraction structure determination and analysis at 1.7 A resolution, solvent-content calculation and molecular-replacement results suggest the presence of two molecules of VioD in the asymmetric unit
Chromobacterium violaceum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Chromobacterium violaceum
enzyme VioD is a flavin-dependent oxygenase that catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein
?
-
-
-
protodeoxyviolaceinate + NAD(P)H + H+ + O2
Chromobacterium violaceum
-
protoviolaceinate + NAD(P)+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, ultrafiltration, and gel filtration
Chromobacterium violaceum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
enzyme VioD is a flavin-dependent oxygenase that catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein
735402
Chromobacterium violaceum
?
-
-
-
-
protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
735402
Chromobacterium violaceum
protoviolaceinate + NAD(P)+
-
-
-
?
General Information
General Information
Commentary
Organism
metabolism
violacein, a natural purple secondary metabolite, is sequentially biosynthesized by five enzymes in the following pathway: VioA-VioB-VioE-VioD-VioC. VioD, a flavin-dependent oxygenase, catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein
Chromobacterium violaceum
General Information (protein specific)
General Information
Commentary
Organism
metabolism
violacein, a natural purple secondary metabolite, is sequentially biosynthesized by five enzymes in the following pathway: VioA-VioB-VioE-VioD-VioC. VioD, a flavin-dependent oxygenase, catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein
Chromobacterium violaceum
Other publictions for EC 1.14.13.217
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)
735402
Ran
Expression, crystallization an ...
Chromobacterium violaceum
Acta crystallogr. Sect. F
71
149-152
2015
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736735
Rodrigues
Systems metabolic engineering ...
Janthinobacterium lividum, Janthinobacterium lividum DSM 1522
Metab. Eng.
20
29-41
2013
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735532
Jiang
Pathway redesign for deoxyviol ...
Duganella sp., Duganella sp. B2
Appl. Microbiol. Biotechnol.
94
1521-1532
2012
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735934
Shinoda
Biosynthesis of violacein: A g ...
Chromobacterium violaceum, Chromobacterium violaceum JCM 1249
Chem. Commun. (Camb.)
2007
4140-4142
2007
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735666
Balibar
In vitro biosynthesis of viola ...
Chromobacterium violaceum, Chromobacterium violaceum ATCC 12472
Biochemistry
45
15444-15457
2006
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735954
Sanchez
Reevaluation of the violacein ...
Chromobacterium violaceum, Chromobacterium violaceum JCM 1249
ChemBioChem
7
1231-1240
2006
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3
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736665
August
Sequence analysis and function ...
Chromobacterium violaceum
J. Mol. Microbiol. Biotechnol.
2
513-519
2000
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