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Literature summary for 1.21.98.2 extracted from
- Evidence for catalytic intermediates involved in generating the chromopyrrolic acid scaffold of rebeccamycin by RebO and RebD (2015), Arch. Biochem. Biophys., 573, 111-119.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| rebD, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Streptomyces sp. |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe | heme protein | Streptomyces sp. |  |
Natural Substrates/ Products (Substrates)
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces sp. | - |
- |
- |
Reaction
| 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 and Products (Substrate)
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| RebD | - |
Streptomyces sp. |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Streptomyces sp. |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Streptomyces sp. |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | a heme-containing peroxidase-like enzyme | Streptomyces sp. | |
General Information
| 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. |
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Release 2023.1 (January 2023)
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