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Literature summary for 1.14.13.217 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
Search for more literature for 1.14.13.217

Cloned(Commentary)

Cloned (Comment) 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] Comment Organism
42000
-
 x * 42000, recombinant His6-tagged enzyme, SDS-PAGE Chromobacterium violaceum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 Comment Textmining
Chromobacterium violaceum Q9S3U8 gene vioD
-
Chromobacterium violaceum ATCC 12472 Q9S3U8 gene vioD
-

Purification (Commentary)

Purification (Comment) 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the recombinant enzyme shows no ability to hydroxylate L-tryptophan. The enzyme does not hydroxylate deoxyviolacein Chromobacterium violaceum ?
-
 ?
additional information the recombinant enzyme shows no ability to hydroxylate L-tryptophan. The enzyme does not hydroxylate deoxyviolacein Chromobacterium violaceum ATCC 12472 ?
-
 ?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
 Chromobacterium violaceum protoviolaceinate + NAD(P)+
-
 ?
protodeoxyviolaceinate + NAD(P)H + H+ + O2 enzyme VioD hydroxylates one indole ring at the 5-position to yield proviolacein Chromobacterium violaceum protoviolaceinate + NAD(P)+
-
 ?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
 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 Chromobacterium violaceum ATCC 12472 protoviolaceinate + NAD(P)+
-
 ?

Subunits

Subunits Comment Organism
? x * 42000, recombinant His6-tagged enzyme, SDS-PAGE Chromobacterium violaceum

Synonyms

Synonyms Comment Organism
VioD
-
 Chromobacterium violaceum

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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

General Information

General Information Comment 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