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Literature summary extracted from

  • Balibar, C.J.; Walsh, C.T.
    In vitro biosynthesis of violacein from L-tryptophan by the enzymes VioA-E from Chromobacterium violaceum (2006), Biochemistry, 45, 15444-15457.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.217 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
1.14.13.224 expression in Escherichia coli Chromobacterium violaceum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.217 42000
-
 x * 42000, recombinant His6-tagged enzyme, SDS-PAGE Chromobacterium violaceum
1.14.13.224 48000
-
 x * 48000, SDS-PAGE Chromobacterium violaceum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.217 protodeoxyviolaceinate + NAD(P)H + H+ + O2 Chromobacterium violaceum enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein protoviolaceinate + NAD(P)+
-
 ?
1.14.13.217 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

EC Number Organism UniProt Comment Textmining
1.14.13.217 Chromobacterium violaceum Q9S3U8 gene vioD
-
1.14.13.217 Chromobacterium violaceum ATCC 12472 Q9S3U8 gene vioD
-
1.14.13.224 Chromobacterium violaceum Q9S3U9
-
-
1.14.13.224 Chromobacterium violaceum DSM 30191 Q9S3U9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.217 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.217 additional information the recombinant enzyme shows no ability to hydroxylate L-tryptophan. The enzyme does not hydroxylate deoxyviolacein Chromobacterium violaceum ?
-
 ?
1.14.13.217 additional information the recombinant enzyme shows no ability to hydroxylate L-tryptophan. The enzyme does not hydroxylate deoxyviolacein Chromobacterium violaceum ATCC 12472 ?
-
 ?
1.14.13.217 protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
 Chromobacterium violaceum protoviolaceinate + NAD(P)+
-
 ?
1.14.13.217 protodeoxyviolaceinate + NAD(P)H + H+ + O2 enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein Chromobacterium violaceum protoviolaceinate + NAD(P)+
-
 ?
1.14.13.217 protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
 Chromobacterium violaceum ATCC 12472 protoviolaceinate + NAD(P)+
-
 ?
1.14.13.217 protodeoxyviolaceinate + NAD(P)H + H+ + O2 enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein Chromobacterium violaceum ATCC 12472 protoviolaceinate + NAD(P)+
-
 ?
1.14.13.224 prodeoxyviolacein + NAD(P)H + O2
-
 Chromobacterium violaceum deoxyviolacein + NAD(P)+ + H2O
-
 ?
1.14.13.224 prodeoxyviolacein + NAD(P)H + O2
-
 Chromobacterium violaceum DSM 30191 deoxyviolacein + NAD(P)+ + H2O
-
 ?
1.14.13.224 proviolacein + NAD(P)H + O2 VioC is able to hydroxylate proviolacein Chromobacterium violaceum violacein + NAD(P)+ + H2O
-
 ?
1.14.13.224 proviolacein + NAD(P)H + O2 VioC is able to hydroxylate proviolacein Chromobacterium violaceum DSM 30191 violacein + NAD(P)+ + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.217 ? x * 42000, recombinant His6-tagged enzyme, SDS-PAGE Chromobacterium violaceum
1.14.13.224 ? x * 48000, SDS-PAGE Chromobacterium violaceum

Synonyms

EC Number Synonyms Comment Organism
1.14.13.217 VioD
-
 Chromobacterium violaceum
1.14.13.224 VioC
-
 Chromobacterium violaceum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.217 22
-
 assay at room temperature Chromobacterium violaceum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.217 9
-
 assay at Chromobacterium violaceum

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.217 FAD a flavin-dependent oxygenase with FAD as bound cofactor Chromobacterium violaceum
1.14.13.217 NADH
-
 Chromobacterium violaceum
1.14.13.217 NADPH
-
 Chromobacterium violaceum
1.14.13.224 FAD
-
 Chromobacterium violaceum
1.14.13.224 NADH
-
 Chromobacterium violaceum
1.14.13.224 NADPH
-
 Chromobacterium violaceum

General Information

EC Number General Information Comment Organism
1.14.13.217 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
1.14.13.224 physiological function flavin-dependent oxygenases, VioC and VioD, act sequentially in biosynthesis of violacein. 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. Deletion of both VioC and VioD leads to formation of a green pigment, deoxychromoviridans, in Top10 cells. When this same construct is transformed into BL21 cells, purple pigment is produced, containing deoxychromoviridans, prodeoxyviolacein, and various other two- and four-electron oxidized versions of prodeoxyviolacein Chromobacterium violaceum