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.
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The expected taxonomic range for this enzyme is: Chromobacterium violaceum
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SYSTEMATIC NAME
IUBMB Comments
protoviolaceinate,NAD(P)H:O2 oxidoreductase
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.
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
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