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EC 1.21.98.2 Details
show Brenda entryEC number
1.21.98.2
Accepted name
dichlorochromopyrrolate synthase
Reaction
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 = dichlorochromopyrrolate + NH3 + 2 H2O
Other name(s)
RebD,
chromopyrrolic acid synthase,
chromopyrrolate synthase
Systematic name
3-(7-chloroindol-3-yl)-2-iminopropanoate ammonia-lyase (dichlorochromopyrrolate-forming)
Comment
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].
History
created 2010 as EC 4.3.1.26, transferred 2013 to EC 1.21.3.9, transferred 2016 to EC 1.21.98.2
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1 Oxidoreductases
1.1.1.70 created 1965, deleted 1978 1.1.1.74 created 1972, deleted 1976 1.1.1.89 created 1972, deleted 1976 1.1.1.109 created 1972, deleted 1976 1.1.1.139 created 1972, deleted 1978 1.1.1.155 created 1976, deleted 2004 1.1.1.171 created 1978, deleted 1984 1.1.1.180 created 1983, deleted 1984 1.1.1.182 created 1983, deleted 1990 1.1.1.204 created 1972 as EC 1.2.1.37, transferred 1984 to EC 1.1.1.204, modified 1989, deleted 2004 1.1.1.242 created 1992, deleted 2001 1.1.1.253 created 1999, deleted 2003
1.1.2 With a cytochrome as acceptor
