PMID:17176066

Balibar CJ, Walsh CT

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

Biochemistry 45:15444-57 (2006)
DOI:10.1021/bi061998z

[cvi:CV_3272]

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

protoviolaceinate,NAD(P)H:O2 oxidoreductase

(1) protoviolaceinate + NAD(P)H + O2 = violaceinate + NAD(P)+ + H2O [RN:R11135 R11373];
(2) protodeoxyviolaceinate + NAD(P)H + O2 = deoxyviolaceinate + NAD(P)+ + H2O [RN:R11132 R11374]

R11132 R11135 R11373 R11374

protoviolaceinate [CPD:C21134];
NADH [CPD:C00004];
NADPH [CPD:C00005];
O2 [CPD:C00007];
protodeoxyviolaceinate [CPD:C21131]

The enzyme, characterized from the bacterium Chromobacterium violaceum, participates in the biosynthesis of the violet pigment violacein. The products, violaceinate and deoxyviolaceinate, undergo non-enzymic autooxidation into violacein and deoxyviolacein, respectively.

EC 1.14.13.224 created 2016

1  [PMID:17176066]

Balibar CJ, Walsh CT

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

Biochemistry 45:15444-57 (2006)
DOI:10.1021/bi061998z

2  [PMID:17925955]

Shinoda K, Hasegawa T, Sato H, Shinozaki M, Kuramoto H, Takamiya Y, Sato T, Nikaidou N, Watanabe T, Hoshino T.

Biosynthesis of violacein: a genuine intermediate, protoviolaceinic acid, produced by VioABDE, and insight into VioC function.

Chem Commun (Camb) 4140-2 (2007)
DOI:10.1039/b705358d

[cvi:CV_3272]