Cloned (Comment) | Organism |
---|---|
rebD, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Streptomyces sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe | heme protein | Streptomyces sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 | Streptomyces sp. | - |
dichlorochromopyrrolate + NH3 + 2 H2O | - |
? | |
additional information | Streptomyces sp. | RebD is a heme-containing peroxidase-like enzyme that catalyzes the oxidative linking of two tryptophan skeletons to form dichlorochromopyrrolic acid. RebD reacts as a peroxidase forming two indole-3-pyruvic acid imine radicals that recombine as a CC bond in the chromopyrrolic acid. When catalase is included to remove H2O2, chromopyrrolic acid can still be formed because the indole-3-pyruvic acid imine rapidly reduces RebD, which reacts with O2, utilizing oxidase-peroxidase chemistry to produce chromopyrrolic acid. Reduced RebD can also react with H2O2 forming Cpd II (state of a hemoprotein that is 1 equivalent of oxidation greater than the ferric form and contains an oxoferryl center) directly, which can oxidize indole-3-pyruvic acid imine. Competitng robust catalase activity of RebD | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces sp. | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 = dichlorochromopyrrolate + NH3 + 2 H2O | peroxidative reaction mechanism for oxidative coupling catalyzed by RebD to form chromopyrrolic acid in the biosynthesis of rebeccamycin, and analysis of the intermediates in the enzyme RebD reaction, overview | Streptomyces sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 | - |
Streptomyces sp. | dichlorochromopyrrolate + NH3 + 2 H2O | - |
? | |
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 | the enzyme performs an unusual biosynthetic step for a hemoprotein in that it forms C-C bonds that link the Trp-derived moieties together | Streptomyces sp. | dichlorochromopyrrolate + NH3 + 2 H2O | - |
? | |
additional information | RebD is a heme-containing peroxidase-like enzyme that catalyzes the oxidative linking of two tryptophan skeletons to form dichlorochromopyrrolic acid. RebD reacts as a peroxidase forming two indole-3-pyruvic acid imine radicals that recombine as a CC bond in the chromopyrrolic acid. When catalase is included to remove H2O2, chromopyrrolic acid can still be formed because the indole-3-pyruvic acid imine rapidly reduces RebD, which reacts with O2, utilizing oxidase-peroxidase chemistry to produce chromopyrrolic acid. Reduced RebD can also react with H2O2 forming Cpd II (state of a hemoprotein that is 1 equivalent of oxidation greater than the ferric form and contains an oxoferryl center) directly, which can oxidize indole-3-pyruvic acid imine. Competitng robust catalase activity of RebD | Streptomyces sp. | ? | - |
? | |
additional information | the enzyme is reduced by indole-3-pyruvic acid imine | Streptomyces sp. | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RebD | - |
Streptomyces sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Streptomyces sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Streptomyces sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | a heme-containing peroxidase-like enzyme | Streptomyces sp. |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is involved in the pathway for the biosynthesis of rebeccamycin, i.e. 1,11-dichloro-12-(4-O-methyl-beta-D-glucopyranosyl)-12,13-dihydro-5H-indolo[2,3-a]pyrrolo[3,4-c]carbazole-5,7(6H)-dione, overview. H2O2 produced from the RebO reaction with Trp to form indole-3-pyruvic acid imine can be used to form Cpd I (state of a hemoprotein that is 2 equivalents of oxidation greater than the ferric form and contains an oxoferryl center (FeIV=O) plus a porphyrin p-cation radical) on RebD, and the Cpd I then via radical chemistry forms the C-C bond that links the tryptophan moieties in chromopyrrolic acid | Streptomyces sp. |