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Literature summary extracted from

  • Howard-Jones, A.R.; Walsh, C.T.
    Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC, and RebC on chromopyrrolic acid (2006), J. Am. Chem. Soc., 128, 12289-12298.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.13.12.17 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(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.17 expression of StaP, StaC, and RebC in Escherichia coli Streptomyces longisporoflavus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.12.17 48000
-
 x * 48000, SDS-PAGE Streptomyces longisporoflavus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.12.17 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+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.17 Streptomyces longisporoflavus Q06IS2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.17
-
 Streptomyces longisporoflavus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.17 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+
-
 ?
1.13.12.17 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+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.12.17 ? x * 48000, SDS-PAGE Streptomyces longisporoflavus

Synonyms

EC Number Synonyms Comment Organism
1.13.12.17 StaP
-
 Streptomyces longisporoflavus

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.12.17 cytochrome P450 StaP is a cytochrome P450 enzyme Streptomyces longisporoflavus
1.13.12.17 Ferredoxin required for activity Streptomyces longisporoflavus
1.13.12.17 NADH NADH is the preferred reductant for StaC- and RebC-mediated turnover of FAD required for activity Streptomyces longisporoflavus