Information on EC 1.21.98.2 - dichlorochromopyrrolate synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.21.98.2
-
RECOMMENDED NAME
GeneOntology No.
dichlorochromopyrrolate synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 = dichlorochromopyrrolate + NH3 + 2 H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
K-252 biosynthesis
-
-
rebeccamycin biosynthesis
-
-
staurosporine biosynthesis
-
-
Staurosporine biosynthesis
-
-
violacein biosynthesis
-
-
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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(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
show the reaction diagram
(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
show the reaction diagram
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2
dichlorochromopyrrolate + NH3 + 2 H2O
show the reaction diagram
2-imino-3-(7-chloroindol-3-yl)propanoate + O2
dichlorochromopyrrolate + NH3 + H2O
show the reaction diagram
4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
show the reaction diagram
7-chloroindole-3-pyruvic acid + 7-chlorotryptophan + O2
11,11'-dichlorochromopyrrolic acid + NH3 + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2
dichlorochromopyrrolate + NH3 + 2 H2O
show the reaction diagram
-
-
-
-
?
4 2-imino-3-(7-chloroindol-3-yl)propanoate + O2
2 dichlorochromopyrrolate + 2 NH3 + 2 H2O
show the reaction diagram
7-chloroindole-3-pyruvic acid + 7-chlorotryptophan + O2
11,11'-dichlorochromopyrrolic acid + NH3 + H2O
show the reaction diagram
additional information
?
-
-
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 C–C 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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
the enzyme contains 2.93 iron centers per polypeptide
additional information
-
does not contain Zn2+, Co2+, Ni2+, Mn2+, Co2+, and Mg2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
-
2 * 56000, SDS-PAGE
110000
-
gel filtration
113000
-
gel filtration, MALDI-TOF mass spectrometry; MALDI-TOF mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, and Superdex 200 gel filtration; purified as a C-terminally His6-tagged protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells; overproduced as a C-terminally His6-tagged protein, expression in Escherichia coli
-
rebD, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-