1A88
CHLOROPEROXIDASE L
Summary for 1A88
| Entry DOI | 10.2210/pdb1a88/pdb |
| Descriptor | CHLOROPEROXIDASE L (2 entities in total) |
| Functional Keywords | haloperoxidase, oxidoreductase |
| Biological source | Streptomyces lividans |
| Total number of polymer chains | 3 |
| Total formula weight | 89448.62 |
| Authors | Hofmann, B.,Toelzer, S.,Pelletier, I.,Altenbuchner, J.,Van Pee, K.-H.,Hecht, H.-J. (deposition date: 1998-04-03, release date: 1998-10-14, Last modification date: 2024-05-22) |
| Primary citation | Hofmann, B.,Tolzer, S.,Pelletier, I.,Altenbuchner, J.,van Pee, K.H.,Hecht, H.J. Structural investigation of the cofactor-free chloroperoxidases. J.Mol.Biol., 279:889-900, 1998 Cited by PubMed 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. PubMed: 9642069DOI: 10.1006/jmbi.1998.1802 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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