1a20

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MOLECULAR MODEL FOR A PLEUROTUS ERYNGII PEROXIDASE OXIDIZING MNII AS WELL AS DIFFERENT PHENOLIC AND NON- PHENOLIC AROMATIC COMPOUNDS AND DYES, THEORETICAL MODELMOLECULAR MODEL FOR A PLEUROTUS ERYNGII PEROXIDASE OXIDIZING MNII AS WELL AS DIFFERENT PHENOLIC AND NON- PHENOLIC AROMATIC COMPOUNDS AND DYES, THEORETICAL MODEL

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed A haem peroxidase different from other microbial, plant and animal peroxidases is described. The enzyme is secreted as two isoforms by dikaryotic Pleurotus eryngii in peptone-containing liquid medium. The corresponding gene, which presents 15 introns and encodes a 361-amino-acid protein with a 30-amino-acid signal peptide, was isolated as two alleles corresponding to the two isoforms. The alleles differ in three amino acid residues and in a seven nucleotide deletion affecting a single metal response element in the promoter. When compared with Phanerochaete chrysosporium peroxidases, the new enzyme appears closer to lignin peroxidase (LiP) than to Mn-dependent peroxidase (MnP) isoenzymes (58-60% and 55% identity respectively). The molecular model built using crystal structures of three fungal peroxidases as templates, also showed high structural affinity with LiP (C alpha-distance 1.2 A). However, this peroxidase includes a Mn2+ binding site formed by three acidic residues (E36, E40 and D175) near the haem internal propionate, which accounts for the ability to oxidize Mn2+. Its capability to oxidize aromatic substrates could involve interactions with aromatic residues at the edge of the haem channel. Another possibility is long-range electron transfer, e.g. from W164, which occupies the same position of LiP W171 recently reported as involved in the catalytic cycle of LiP. Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii.,Ruiz-Duenas FJ, Martinez MJ, Martinez AT Mol Microbiol. 1999 Jan;31(1):223-35. PMID:9987124 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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