1.14.13.217: protodeoxyviolaceinate monooxygenase
This is an abbreviated version!
For detailed information about protodeoxyviolaceinate monooxygenase, go to the full flat file.
Reaction
Synonyms
protoviolaceinate synthase, VioD, VioD oxygenase
ECTree
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General Information on EC 1.14.13.217 - protodeoxyviolaceinate monooxygenase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
metabolism
physiological function
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genes vioA, vioC and vioD encode nucleotide-dependent monooxygenases
evolution
VioD belongs to the family of flavin-containing NAD(P)H-dependent monooxygenases
evolution
Chromobacterium violaceum JCM 1249
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VioD belongs to the family of flavin-containing NAD(P)H-dependent monooxygenases
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malfunction
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biosynthetic pathway of L-tryptophan to violacein in the wild-type and and deoxyviolacein in the vioD deletion mutant, overview
malfunction
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disruption of vioA or vioB completely abrogates the biosynthesis of violacein intermediates, while disruption of the vioC or vioD genes results in the production of violacein precursors
malfunction
disruption of vioA or vioB completely abrogates the biosynthesis of violacein intermediates, while disruption of vioC or vioD results in the production of violacein precursors. Gene vioE is essential for violacein biosynthesis. Enzymes VioC and VioD are responsible for the oxygenations at the ox-indole and hydroxyindole, respectively. In the absence of VioC, the expected proviolaceins are accompanied by other compounds: deoxychromoviridans, chromoviridans, and oxychromoviridans
malfunction
formation of deoxyviolacein and prodeoxyviolacein occurs due to the insufficient amount of VioD
malfunction
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biosynthetic pathway of L-tryptophan to violacein in the wild-type and and deoxyviolacein in the vioD deletion mutant, overview
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malfunction
Chromobacterium violaceum JCM 1249
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formation of deoxyviolacein and prodeoxyviolacein occurs due to the insufficient amount of VioD
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malfunction
Chromobacterium violaceum JCM 1249
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disruption of vioA or vioB completely abrogates the biosynthesis of violacein intermediates, while disruption of vioC or vioD results in the production of violacein precursors. Gene vioE is essential for violacein biosynthesis. Enzymes VioC and VioD are responsible for the oxygenations at the ox-indole and hydroxyindole, respectively. In the absence of VioC, the expected proviolaceins are accompanied by other compounds: deoxychromoviridans, chromoviridans, and oxychromoviridans
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metabolism
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biosynthetic pathway of L-tryptophan to violacein in the wild-type and and deoxyviolacein in the vioD deletion mutant, NMR analysis of reactio products and intermediates, overview
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
metabolism
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the enzyme is involved in the violacein biosynthetic pathway from Chromobacterium violaceum, sequence analysis and functional characterization, overview. The four genes vioABCD are necessary for violacein production
metabolism
the enzyme is involved in the violacein biosynthetic pathway, which is proposed to consist of the reactions of enzymes VioA -> VioB -> VioE -> VioD -> VioC
metabolism
vioD is one gene encoding violacein biosynthesis, VioD appears to act on late steps of violacein biosynthesis, overview
metabolism
violacein, a natural purple secondary metabolite, is sequentially biosynthesized by five enzymes in the following pathway: VioA-VioB-VioE-VioD-VioC. VioD, a flavin-dependent oxygenase, catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein
metabolism
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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
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metabolism
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biosynthetic pathway of L-tryptophan to violacein in the wild-type and and deoxyviolacein in the vioD deletion mutant, NMR analysis of reactio products and intermediates, overview
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metabolism
Chromobacterium violaceum JCM 1249
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the enzyme is involved in the violacein biosynthetic pathway, which is proposed to consist of the reactions of enzymes VioA -> VioB -> VioE -> VioD -> VioC
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metabolism
Chromobacterium violaceum JCM 1249
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vioD is one gene encoding violacein biosynthesis, VioD appears to act on late steps of violacein biosynthesis, overview
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