1.21.98.2: dichlorochromopyrrolate synthase

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For detailed information about dichlorochromopyrrolate synthase, go to the full flat file.

Reaction

2 3-(7-chloroindol-3-yl)-2-iminopropanoate +

Synonyms

EC 1.21.3.9, EC 4.3.1.26, RebD

ECTree

     1 Oxidoreductases

         1.21 Catalysing the reaction X-H + Y-H = X-Y

             1.21.98 With other, known, physiological acceptors

                1.21.98.2 dichlorochromopyrrolate synthase

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Results	in table
28	AA Sequence
4	Cloned(Commentary)
7	Cofactor
3	General Information
4	Metals/Ions
4	Molecular Weight [Da]
8	Natural Substrates/ Products (Substrates)
13	Organism
9	Pathway
1	pH Optimum
2	Purification (Commentary)
2	Reaction
7	Reference
26	Substrates and Products (Substrate)
4	Subunits
8	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]

Systematic Name

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Systematic Name on EC 1.21.98.2 - dichlorochromopyrrolate synthase

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SYSTEMATIC NAME

IUBMB Comments

3-(7-chloroindol-3-yl)-2-iminopropanoate ammonia-lyase (dichlorochromopyrrolate-forming)

This 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 [1]. Contains one molecule of heme b per monomer, as well as non-heme iron that is not part of an iron-sulfur center [2]. 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 [3].