Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | StaP, a cytochrome P450 enzyme, catalyzes an aryl-aryl bond-forming reaction to give a six-ring indolocarbazole scaffold, as well as mediating decarboxylation and oxidation of the putative dicarboxypyrrole moiety. This action requires two to four cycles of net two-electron substrate oxidation at the catalytic heme center. StaP produces three distinct products, differing in oxidation level. For the production of K252c from chromopyrrolic acid, a net four-electron oxidation is required. The generation ofarcyriaflavin A from chromopyrrolic acid requires an overall eight-electron oxidation. StaP is thus unusual in the apparent lack of oxidative control it possesses over the outcome of its catalytic turnover. Control of the overall oxidation route is provided by a second enzyme StaC, which imparts the net effect of directing the oxidation level of the pyrrole-derived ring. While StaP in isolation gives three aglycone forms, StaP and StaC turn over chromopyrrolic acid to give only a single product, K252c. Similarly, RebC guides the turnover of chromopyrrolic acid toward the more highly oxidized maleimide-bearing aglycone, arcyriaflavin A | Streptomyces longisporoflavus |
Cloned (Comment) | Organism |
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expression of StaP, StaC, and RebC in Escherichia coli | Streptomyces longisporoflavus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
48000 | - |
x * 48000, SDS-PAGE | Streptomyces longisporoflavus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dichlorochromopyrrolate + 4 O2 + 4 NADH + 4 H+ | Streptomyces longisporoflavus | the reaction is catalyzed by enzyme StaP. StaC and RebC acting to direct the level of oxidation in the newly formed five-membered ring. Biosynthesis of the antitumor indolocarbazoles rebeccamycin and staurosporine by streptomycetes | 1,11-dichloroarcyriaflavin A + 2 CO2 + 6 H2O + 4 NAD+ | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces longisporoflavus | Q06IS2 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Streptomyces longisporoflavus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dichlorochromopyrrolate + 4 O2 + 4 NADH + 4 H+ | the reaction is catalyzed by enzyme StaP. StaC and RebC acting to direct the level of oxidation in the newly formed five-membered ring. Biosynthesis of the antitumor indolocarbazoles rebeccamycin and staurosporine by streptomycetes | Streptomyces longisporoflavus | 1,11-dichloroarcyriaflavin A + 2 CO2 + 6 H2O + 4 NAD+ | - |
? | |
dichlorochromopyrrolate + 4 O2 + 4 NADH + 4 H+ | StaP, a cytochrome P450 enzyme, catalyzes an aryl-aryl bond-forming reaction to give a six-ring indolocarbazole scaffold, as well as mediating decarboxylation and oxidation of the putative dicarboxypyrrole moiety. This action requires two to four cycles of net two-electron substrate oxidation at the catalytic heme center. StaP produces three distinct products, differing in oxidation level. For the production of K252c from chromopyrrolic acid, a net four-electron oxidation is required. The generation ofarcyriaflavin A from chromopyrrolic acid requires an overall eight-electron oxidation. StaP is thus unusual in the apparent lack of oxidative control it possesses over the outcome of its catalytic turnover. Control of the overall oxidation route is provided by a second enzyme StaC, which imparts the net effect of directing the oxidation level of the pyrrole-derived ring. While StaP in isolation gives three aglycone forms, StaP and StaC turn over chromopyrrolic acid to give only a single product, K252c. Similarly, RebC (flavin-dependent hydroxylase) guides the turnover of chromopyrrolic acid toward the more highly oxidized maleimide-bearing aglycone, arcyriaflavin A | Streptomyces longisporoflavus | 1,11-dichloroarcyriaflavin A + 2 CO2 + 6 H2O + 4 NAD+ | - |
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Subunits | Comment | Organism |
---|---|---|
? | x * 48000, SDS-PAGE | Streptomyces longisporoflavus |
Synonyms | Comment | Organism |
---|---|---|
StaP | - |
Streptomyces longisporoflavus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome P450 | StaP is a cytochrome P450 enzyme | Streptomyces longisporoflavus | |
Ferredoxin | required for activity | Streptomyces longisporoflavus | |
NADH | NADH is the preferred reductant for StaC- and RebC-mediated turnover of FAD required for activity | Streptomyces longisporoflavus |