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IUBMB CommentsThis enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. The enzyme is a dimeric heme-protein oxidase that catalyses the oxidative dimerization of two L-tryptophan-derived molecules to form dichlorochromopyrrolic acid, the precursor for the fused six-ring indolocarbazole scaffold of rebeccamycin . Contains one molecule of heme b per monomer, as well as non-heme iron that is not part of an iron-sulfur center . In vivo the enzyme uses hydrogen peroxide, formed by the enzyme upstream in the biosynthetic pathway (EC 1.4.3.23, 7-chloro-L-tryptophan oxidase) as the electron acceptor. However, the enzyme is also able to catalyse the reaction using molecular oxygen .
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(2E)-2-[(E)-[1-carboxy-2-(1H-indol-3-yl)ethylidene]amino]-3-(2,3-dihydro-1H-indol-3-yl)prop-2-enoic acid + O2
3-(2,3-dihydro-1H-indol-3-yl)-4-(1H-indol-3-yl)-1H-pyrrole-2,5-dicarboxylic acid + NH3 + H2O
(2E)-2-[(E)-[1-carboxy-2-(7-chloro-1H-indol-3-yl)ethylidene]amino]-3-(7-chloro-2,3-dihydro-1H-indol-3-yl)prop-2-enoic acid + O2
3-(7-chloro-2,3-dihydro-1H-indol-3-yl)-4-(7-chloro-1H-indol-3-yl)-1H-pyrrole-2,5-dicarboxylic acid + NH3 + H2O
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2
dichlorochromopyrrolate + NH3 + 2 H2O
2-imino-3-(7-chloroindol-3-yl)propanoate + O2
dichlorochromopyrrolate + NH3 + H2O
4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
7-chloroindole-3-pyruvic acid + 7-chlorotryptophan + O2
11,11'-dichlorochromopyrrolic acid + NH3 + H2O
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(2E)-2-[(E)-[1-carboxy-2-(1H-indol-3-yl)ethylidene]amino]-3-(2,3-dihydro-1H-indol-3-yl)prop-2-enoic acid + O2
3-(2,3-dihydro-1H-indol-3-yl)-4-(1H-indol-3-yl)-1H-pyrrole-2,5-dicarboxylic acid + NH3 + H2O
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(2E)-2-[(E)-[1-carboxy-2-(1H-indol-3-yl)ethylidene]amino]-3-(2,3-dihydro-1H-indol-3-yl)prop-2-enoic acid + O2
3-(2,3-dihydro-1H-indol-3-yl)-4-(1H-indol-3-yl)-1H-pyrrole-2,5-dicarboxylic acid + NH3 + H2O
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(2E)-2-[(E)-[1-carboxy-2-(7-chloro-1H-indol-3-yl)ethylidene]amino]-3-(7-chloro-2,3-dihydro-1H-indol-3-yl)prop-2-enoic acid + O2
3-(7-chloro-2,3-dihydro-1H-indol-3-yl)-4-(7-chloro-1H-indol-3-yl)-1H-pyrrole-2,5-dicarboxylic acid + NH3 + H2O
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(2E)-2-[(E)-[1-carboxy-2-(7-chloro-1H-indol-3-yl)ethylidene]amino]-3-(7-chloro-2,3-dihydro-1H-indol-3-yl)prop-2-enoic acid + O2
3-(7-chloro-2,3-dihydro-1H-indol-3-yl)-4-(7-chloro-1H-indol-3-yl)-1H-pyrrole-2,5-dicarboxylic acid + NH3 + H2O
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2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2
dichlorochromopyrrolate + NH3 + 2 H2O
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2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2
dichlorochromopyrrolate + NH3 + 2 H2O
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the enzyme performs an unusual biosynthetic step for a hemoprotein in that it forms C-C bonds that link the Trp-derived moieties together
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2-imino-3-(7-chloroindol-3-yl)propanoate + O2
dichlorochromopyrrolate + NH3 + H2O
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2-imino-3-(7-chloroindol-3-yl)propanoate + O2
dichlorochromopyrrolate + NH3 + H2O
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4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
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4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
rebeccamycin biosynthetic pathway
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4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
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4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
rebeccamycin biosynthetic pathway
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4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
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4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
rebeccamycin biosynthetic pathway
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7-chloroindole-3-pyruvic acid + 7-chlorotryptophan + O2
11,11'-dichlorochromopyrrolic acid + NH3 + H2O
RebD is involved in the construction of a bisindole structure by catalyzing a coupling reaction between 7-chlorotryptophan and 7-chloroindole-3-pyruvic acid
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7-chloroindole-3-pyruvic acid + 7-chlorotryptophan + O2
11,11'-dichlorochromopyrrolic acid + NH3 + H2O
RebD is involved in the construction of a bisindole structure by catalyzing a coupling reaction between 7-chlorotryptophan and 7-chloroindole-3-pyruvic acid
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RebD acts as an efficient catalase, effecting the disproportionation of hydrogen peroxide to give oxygen and water
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the enzyme has both catalase and chromopyrrolic acid synthase activity. The enzyme acts as an efficient catalase, effecting the disproportionation of hydrogen peroxide to give oxygen and (presumably) water. The enzyme on its own is incompetent with L-tryptophan
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RebD acts as an efficient catalase, effecting the disproportionation of hydrogen peroxide to give oxygen and water
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the enzyme has both catalase and chromopyrrolic acid synthase activity. The enzyme acts as an efficient catalase, effecting the disproportionation of hydrogen peroxide to give oxygen and (presumably) water. The enzyme on its own is incompetent with L-tryptophan
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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
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the enzyme is reduced by indole-3-pyruvic acid imine
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2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2
dichlorochromopyrrolate + NH3 + 2 H2O
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4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
7-chloroindole-3-pyruvic acid + 7-chlorotryptophan + O2
11,11'-dichlorochromopyrrolic acid + NH3 + H2O
additional information
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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
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4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
rebeccamycin biosynthetic pathway
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4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
rebeccamycin biosynthetic pathway
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7-chloroindole-3-pyruvic acid + 7-chlorotryptophan + O2
11,11'-dichlorochromopyrrolic acid + NH3 + H2O
RebD is involved in the construction of a bisindole structure by catalyzing a coupling reaction between 7-chlorotryptophan and 7-chloroindole-3-pyruvic acid
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7-chloroindole-3-pyruvic acid + 7-chlorotryptophan + O2
11,11'-dichlorochromopyrrolic acid + NH3 + H2O
RebD is involved in the construction of a bisindole structure by catalyzing a coupling reaction between 7-chlorotryptophan and 7-chloroindole-3-pyruvic acid
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Howard-Jones, A.R.; Walsh, C.T.
Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD
Biochemistry
44
15652-15663
2005
Lentzea aerocolonigenes (Q8KHV6), Lentzea aerocolonigenes ATCC 39243 (Q8KHV6)
brenda
Nishizawa, T.; Grschow, S.; Jayamaha, D.H.; Nishizawa-Harada, C.; Sherman, D.H.
Enzymatic assembly of the bis-indole core of rebeccamycin
J. Am. Chem. Soc.
128
724-725
2006
Lentzea aerocolonigenes (Q8KHV6), Lentzea aerocolonigenes ATCC 39243 (Q8KHV6)
brenda
Onaka, H.; Taniguchi, S.; Igarashi, Y.; Furumai, T.
Characterization of the biosynthetic gene cluster of rebeccamycin from Lechevalieria aerocolonigenes ATCC 39243
Biosci. Biotechnol. Biochem.
67
127-138
2003
Lentzea aerocolonigenes (Q8KHV6), Lentzea aerocolonigenes ATCC 39243 (Q8KHV6)
brenda
Spolitak, T.; Ballou, D.P.
Evidence for catalytic intermediates involved in generating the chromopyrrolic acid scaffold of rebeccamycin by RebO and RebD
Arch. Biochem. Biophys.
573
111-119
2015
Streptomyces sp.
brenda
Enzyme Nomenclature
1.21.98.2 dichlorochromopyrrolate synthase
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