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Literature summary for 1.14.13.217 extracted from

  • Ran, T.; Gao, M.; Wei, Q.; He, J.; Tang, L.; Wang, W.; Xu, D.
    Expression, crystallization and preliminary crystallographic data analysis of VioD, a hydroxylase in the violacein-biosynthesis pathway (2015), Acta crystallogr. Sect. F, 71, 149-152.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene vioD, recombinant expression of His-tagged enzyme in Escherichia coli Chromobacterium violaceum

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 7.5-15 mg/ml protein in 20 mM Tris–HCl pH 8.0, 300 mM NaCl, 10% glycerol, with 0.001 ml of reservoir solution containing 3.5 M sodium formate pH 7.0, and equilibration against 0.05 ml of reservoir solution, 2 weeks, X-ray diffraction structure determination and analysis at 1.7 A resolution, solvent-content calculation and molecular-replacement results suggest the presence of two molecules of VioD in the asymmetric unit Chromobacterium violaceum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Chromobacterium violaceum enzyme VioD is a flavin-dependent oxygenase that catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein ?
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2 Chromobacterium violaceum
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protoviolaceinate + NAD(P)+
-
?

Organism

Organism UniProt Comment Textmining
Chromobacterium violaceum A0A024AX32
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, ultrafiltration, and gel filtration Chromobacterium violaceum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme VioD is a flavin-dependent oxygenase that catalyzes the hydroxylation of the intermediate product prodeoxyviolaceinic acid at the 5-position of one indole ring to yield proviolacein Chromobacterium violaceum ?
-
?
protodeoxyviolaceinate + NAD(P)H + H+ + O2
-
Chromobacterium violaceum protoviolaceinate + NAD(P)+
-
?

Synonyms

Synonyms Comment Organism
VioD
-
Chromobacterium violaceum

Cofactor

Cofactor Comment Organism Structure
NADH
-
Chromobacterium violaceum
NADPH
-
Chromobacterium violaceum

General Information

General Information Comment Organism
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 Chromobacterium violaceum