Detail Information for IndEnz0007000111
IED ID IndEnz0007000111
Enzyme Type ID catalase000111
Protein Name Dichlorochromopyrrolate synthase
EC 1.21.98.2
Catalase
EC 1.11.1.6
Gene Name rebD rbmC
Organism Lentzea aerocolonigenes (Lechevalieria aerocolonigenes) (Saccharothrix aerocolonigenes)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Pseudonocardiales Pseudonocardiaceae Lentzea Lentzea aerocolonigenes (Lechevalieria aerocolonigenes) (Saccharothrix aerocolonigenes)
Enzyme Sequence MSVFDLPRLHFAGTATTRLPTGPRNGLVDLSTHSVVMDGERFPASRPAAEYHAYLDRVGGKGTAFAGNGYFAIDAGITAVERAAGEVDTGDLLVGRAVDVWGHYNEYLATTFNRARIFDVDPSSSWTSTVMIGQFGFGRLGRSHDVGYVFTGGVHGMQPPRWHEDGRVLHQFTVPAGEDMTWFGSAADSPAAARLRELVESGEADGLVVQLALSDAGPAPMPHAQQWRLRGTIAPWHAGEPRTCPAGRLLTPHNLTADLRGDHVSLNLISFRPPTGISGLELRTADTDRFIARVPADDPHGVVTVPAAEGGDEALCVVGTTAAGERIVVSREREVTVHVDDASVFLEHPRGPGDSDQDAEIAVRTYVRGEPAAATIHIGQYFNPRAFPLDEHATAASATPEDLDVVALCVDGTRWSRHCVISTDENGDGRFLLRGARPGATRLLLSAEGATPFDGLTAAAAYDNDDSLGLWSGLASVAVRVLPDHWWMDDIPRDKVTFDLLYREVFAFYELLYSFMGEEVFSLADRFRVETHPRLIWQMCDPRNRAKTYYMPPTRDLTGPQARLLLAYLRAQNSDVVVPVIEPSHTRSGTPISTRTDLVRALRHGVAIELAVMLQYLYAAFSIPTHGAGQELVSRGDWTPEQLRLMCGDGGETTDGGVRGSLLGVAREEMIHFLVVNNVLMAVGEPFHVPDLDFGTINDTLMVPLDFSLEALGLGSVQRFIQIEQPEGLTGAVRLGDLPVPVREAEDFHYASLSELYGDIREGLQRVPGLFLVERGRGGGEHHLFLRESVNAVHPDYQLEVDDLSSALFAIDFVTEQGEGHVLTDEDTGEESHYDTFVRVADLLMKERLTAADTRRAQWSPAYPVARNPTVHGGGQSKELVTSPVARELMVLFNKSYFMMLQLMVQHFGGSPDASLRRSKLMNAAIDVMTGVMRPLAELLVTVPSGRHGRTAGPSFELDEKPAFIPRADVARRAISLRFRHLAESARTCALVPDKVVRNLDFLADQFATEGPR
Enzyme Length 1013
Uniprot Accession Number Q8KHV6
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H2O2 = dichlorochromopyrrolate + H(+) + 2 H2O + NH4(+); Xref=Rhea:RHEA:27393, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:59194, ChEBI:CHEBI:59198; EC=1.21.98.2; Evidence={ECO:0000269|PubMed:16313168, ECO:0000269|PubMed:25837855}; CATALYTIC ACTIVITY: Reaction=2 2-iminio-3-(indol-3-yl)propanoate + H2O2 = chromopyrrolate + H(+) + 2 H2O + NH4(+); Xref=Rhea:RHEA:50920, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:59193, ChEBI:CHEBI:133898; EC=1.21.98.2; Evidence={ECO:0000269|PubMed:25837855}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000269|PubMed:16313168};
DNA Binding
EC Number 1.21.98.2; 1.11.1.6
Enzyme Function FUNCTION: Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyzes the hydrogen peroxide-dependent dimerization of two L-tryptophan-derived molecules (imine form of indole 3-pyruvate (IPA)), to form dichlorochromopyrrolic acid (CPA), the precursor for the six-ring bisindolopyrrolocarbazole scaffold of the rebeccamycin. The hydrogen peroxide is provided together with iminoindolpropanoate by RebO. Due to the instability of indole 3-pyruvate (IPA), which is hydrolyzed in solution and exits in equilibrium with the predominant ketone form of IPA, the concerted functioning of the RebO/RebD system appears to prevent the buildup of significant amounts of IPA and its imine in solution, effectively shepherding the imine further down the biosynthetic chain. {ECO:0000269|PubMed:12619684, ECO:0000269|PubMed:16313168, ECO:0000269|PubMed:25837855}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1)
Keywords Heme;Iron;Metal-binding;Oxidoreductase
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 110,746
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 mM for 2-imino-3-(indol-3-yl)propanoate (at pH 7.5) {ECO:0000269|PubMed:16313168}; Note=kcat is 64000 min(-1) for 2-imino-3-(indol-3-yl)propanoate (at pH 7.5).;
Metal Binding
Rhea ID RHEA:27393; RHEA:50920; RHEA:20309
Cross Reference Brenda 1.21.98.2;