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 Maximum [Da] | Comment | Organism |
---|---|---|---|
42000 | - |
x * 42000, recombinant His6-tagged enzyme, SDS-PAGE | Chromobacterium violaceum |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Chromobacterium violaceum | Q9S3U8 | gene vioD | - |
Chromobacterium violaceum ATCC 12472 | Q9S3U8 | gene vioD | - |
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 | 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 | Comment | Organism |
---|---|---|
? | x * 42000, recombinant His6-tagged enzyme, SDS-PAGE | Chromobacterium violaceum |
Synonyms | Comment | Organism |
---|---|---|
VioD | - |
Chromobacterium violaceum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Chromobacterium violaceum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
assay at | Chromobacterium violaceum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | a flavin-dependent oxygenase with FAD as bound cofactor | Chromobacterium violaceum | |
NADH | - |
Chromobacterium violaceum | |
NADPH | - |
Chromobacterium violaceum |
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 |