Structural highlights
Function
[BPA1_STRAU] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural investigation of the cofactor-free chloroperoxidases.,Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:9642069[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ. Structural investigation of the cofactor-free chloroperoxidases. J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:9642069 doi:http://dx.doi.org/10.1006/jmbi.1998.1802
