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==

== Structural highlights ==

<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A20 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a20 FirstGlance], [http://www.ebi.ac.uk/pdbsum/1a20 PDBsum]</span></td></tr>

<table>

== 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.

~~[[Image~~:~~1a20~~.~~png|left|200px]]~~

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>

~~{{STRUCTURE_1a20| PDB=1a20 | SCENE= }}~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

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

== References ==

~~{{ABSTRACT_PUBMED_9987124}}~~

__TOC__

</StructureSection>

==~~Reference~~==

<~~ref group="xtra">PMID:009987124<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: Martinez, A T]]

[[Category: Martinez, M J]]

[[Category: Romero, A]]

[[Category: Ruiz-Duenas, F J]]

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@@ Line 1: / Line 1: @@
-{{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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A20 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a20 FirstGlance], [http://www.ebi.ac.uk/pdbsum/1a20 PDBsum]</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.
-[[Image:1a20.png|left|200px]]
+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>
-{{STRUCTURE_1a20|  PDB=1a20  |  SCENE=  }}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-===MOLECULAR MODEL FOR A PLEUROTUS ERYNGII PEROXIDASE OXIDIZING MNII AS WELL AS DIFFERENT PHENOLIC AND NON- PHENOLIC AROMATIC COMPOUNDS AND DYES, THEORETICAL MODEL===
+== References ==
+<references/>
-{{ABSTRACT_PUBMED_9987124}}
+__TOC__
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:009987124</ref><references group="xtra"/>
 [[Category: Martinez, A T]]
 [[Category: Martinez, M J]]
 [[Category: Romero, A]]
 [[Category: Ruiz-Duenas, F J]]