Gene_locus Report for: strau-cpoT

Kitasatospora aureofaciens Streptomyces aureofaciens non-haem chloroperoxidase (cpoT)

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > Terrabacteria group: N E > Actinobacteria [phylum]: N E > Actinobacteria [class]: N E > Streptomycetales: N E > Streptomycetaceae: N E > Kitasatospora: N E > Kitasatospora aureofaciens: N E

Abhydrolase_9 : strau-a0a0l8p583Streptomyces aureofaciens; Streptomyces rimosus; Streptomyces sp.; Streptomyces albus, Membrane protein, strau-a0a0l8q9h5Streptomyces aureofaciens; Streptomyces griseoflavus; Streptomyces rimosus; Streptomyces sp.; Streptomyces albus Membrane protein.
Chlorophyllase : strau-a0a1e7n9b6Streptomyces aureofaciens. Chlorophyllase.
Duf_1023 : strau-a0a0l8pd36Streptomyces aureofaciens, Uncharacterized protein, strau-a0a176sa95Streptomyces aureofaciens, Uncharacterized protein, strau-a0a176saa3Streptomyces aureofaciens, Uncharacterized protein, strau-a0a176sdb0Streptomyces aureofaciens, Uncharacterized protein, strau-a0a176sdj6Streptomyces aureofaciens, Uncharacterized protein, strau-a0a176sft8Streptomyces aureofaciens, Uncharacterized protein, strau-a0a176sgc2Streptomyces aureofaciens, Uncharacterized protein.
Haloperoxidase : strau-brpa1 Streptomyces aureofaciens bromoperoxidase BPO-A1 (bpoA1), strau-brpa2 Streptomyces aureofaciens metal-ion-free oxidoreductase (bpo2), bromoperoxidase, chloroperoxidase CPO-A2 (cpoA2).
Thioesterase : strau-q30cr8Streptomyces aureofaciens lipte

Title: Structural investigation of the cofactor-free chloroperoxidases
Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ
Ref: Journal of Molecular Biology, 279:889, 1998 : PubMed
Abstract


ESTHER: Hofmann_1998_J.Mol.Biol_279_889
PubMedSearch: Hofmann 1998 J.Mol.Biol 279 889
PubMedID: 9642069
Gene_locus related to this paper: psefl-cpoF, strau-brpa2, strau-cpoT, strli-cpoL
Inhibitor(s) related to this paper: Benzoic-acid

Abstract

The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens, Streptomyces lividans, and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites.