BRENDA - Enzyme Database
show all sequences of 1.14.13.217

In vitro biosynthesis of violacein from L-tryptophan by the enzymes VioA-E from Chromobacterium violaceum

Balibar, C.J.; Walsh, C.T.; Biochemistry 45, 15444-15457 (2006)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene vioD, reconstruction of the violacein biosynthesis pathway in Escherichia coli strain BL21 (DE3), recombinant expression of the C-terminally His6-tagged enzyme
Chromobacterium violaceum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
x * 42000, recombinant His6-tagged enzyme, SDS-PAGE
Chromobacterium violaceum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
protodeoxyviolaceinate + NAD(P)H + H+ + O2
Chromobacterium violaceum
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
protoviolaceinate + NAD(P)+
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
Chromobacterium violaceum ATCC 12472
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
protoviolaceinate + NAD(P)+
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Chromobacterium violaceum
Q9S3U8
gene vioD
-
Chromobacterium violaceum ATCC 12472
Q9S3U8
gene vioD
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) to homogeneity by nickel affinity chromatography and gel filtration in tandem
Chromobacterium violaceum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
the recombinant enzyme shows no ability to hydroxylate L-tryptophan. The enzyme does not hydroxylate deoxyviolacein
735666
Chromobacterium violaceum
?
-
-
-
-
additional information
the recombinant enzyme shows no ability to hydroxylate L-tryptophan. The enzyme does not hydroxylate deoxyviolacein
735666
Chromobacterium violaceum ATCC 12472
?
-
-
-
-
protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
735666
Chromobacterium violaceum
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
735666
Chromobacterium violaceum
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
735666
Chromobacterium violaceum ATCC 12472
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
735666
Chromobacterium violaceum ATCC 12472
protoviolaceinate + NAD(P)+
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 42000, recombinant His6-tagged enzyme, SDS-PAGE
Chromobacterium violaceum
Synonyms
Synonyms
Commentary
Organism
VioD
-
Chromobacterium violaceum
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at room temperature
Chromobacterium violaceum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Chromobacterium violaceum
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
a flavin-dependent oxygenase with FAD as bound cofactor
Chromobacterium violaceum
NADH
-
Chromobacterium violaceum
NADPH
-
Chromobacterium violaceum
Cloned(Commentary) (protein specific)
Commentary
Organism
gene vioD, reconstruction of the violacein biosynthesis pathway in Escherichia coli strain BL21 (DE3), recombinant expression of the C-terminally His6-tagged enzyme
Chromobacterium violaceum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
a flavin-dependent oxygenase with FAD as bound cofactor
Chromobacterium violaceum
NADH
-
Chromobacterium violaceum
NADPH
-
Chromobacterium violaceum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
x * 42000, recombinant His6-tagged enzyme, SDS-PAGE
Chromobacterium violaceum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
protodeoxyviolaceinate + NAD(P)H + H+ + O2
Chromobacterium violaceum
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
protoviolaceinate + NAD(P)+
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
Chromobacterium violaceum ATCC 12472
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
protoviolaceinate + NAD(P)+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) to homogeneity by nickel affinity chromatography and gel filtration in tandem
Chromobacterium violaceum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
the recombinant enzyme shows no ability to hydroxylate L-tryptophan. The enzyme does not hydroxylate deoxyviolacein
735666
Chromobacterium violaceum
?
-
-
-
-
additional information
the recombinant enzyme shows no ability to hydroxylate L-tryptophan. The enzyme does not hydroxylate deoxyviolacein
735666
Chromobacterium violaceum ATCC 12472
?
-
-
-
-
protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
735666
Chromobacterium violaceum
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
735666
Chromobacterium violaceum
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
735666
Chromobacterium violaceum ATCC 12472
protoviolaceinate + NAD(P)+
-
-
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein
735666
Chromobacterium violaceum ATCC 12472
protoviolaceinate + NAD(P)+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 42000, recombinant His6-tagged enzyme, SDS-PAGE
Chromobacterium violaceum
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at room temperature
Chromobacterium violaceum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Chromobacterium violaceum
General Information
General Information
Commentary
Organism
metabolism
the biosynthesis of violacein from 2 molecules of L-tryptophan requires five contiguously encoded proteins VioA-E. VioC and VioD act sequentially, VioD hydroxylates one indole ring at the 5-position to yield proviolacein, and VioC then acts on the other indole ring at the 2-position to create the oxindole and complete violacein formation. the order of hydroxylation on route to violacein is VioD followed by VioC. L-tryptophan, and not 5-hydroxy-L-tryptophan, is the sole precursor to violacein
Chromobacterium violaceum
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the biosynthesis of violacein from 2 molecules of L-tryptophan requires five contiguously encoded proteins VioA-E. VioC and VioD act sequentially, VioD hydroxylates one indole ring at the 5-position to yield proviolacein, and VioC then acts on the other indole ring at the 2-position to create the oxindole and complete violacein formation. the order of hydroxylation on route to violacein is VioD followed by VioC. L-tryptophan, and not 5-hydroxy-L-tryptophan, is the sole precursor to violacein
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
Synonyms
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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1
1
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2
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1
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1
2
1
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1
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2
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1
1
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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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1
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2
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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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1
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2
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2
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2
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1
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2
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1
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2
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2
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2
2
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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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2
2
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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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1
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1
2
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2
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1
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6
1
1
1
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1
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3
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1
3
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2
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1
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6
1
1
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1
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1
1
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-
735954
Sanchez
Reevaluation of the violacein ...
Chromobacterium violaceum, Chromobacterium violaceum JCM 1249
ChemBioChem
7
1231-1240
2006
1
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1
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1
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4
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3
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4
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2
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2
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1
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1
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4
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4
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3
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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3
3
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