1a20: Difference between revisions
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{{Theoretical_model}} | |||
==MOLECULAR MODEL FOR A PLEUROTUS ERYNGII PEROXIDASE OXIDIZING MNII AS WELL AS DIFFERENT PHENOLIC AND NON- PHENOLIC AROMATIC COMPOUNDS AND DYES, THEORETICAL MODEL== | |||
<StructureSection load='1a20' size='340' side='right'caption='[[1a20]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A20 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a20 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1a20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a20 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:9987124</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 1a20" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Martinez, A T]] | |||
[[Category: Martinez, M J]] | |||
[[Category: Romero, A]] | |||
[[Category: Ruiz-Duenas, F J]] | |||