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| | ==Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.9 A== | | ==Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.9 A== |
| - | <StructureSection load='5whq' size='340' side='right' caption='[[5whq]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='5whq' size='340' side='right'caption='[[5whq]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5whq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neucr Neucr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WHQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5whq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa_OR74A Neurospora crassa OR74A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WHQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5whs|5whs]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">katG, cat-2, NCU05770 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=367110 NEUCR])</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=5whq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5whq OCA], [https://pdbe.org/5whq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5whq RCSB], [https://www.ebi.ac.uk/pdbsum/5whq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5whq ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase_peroxidase Catalase peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.21 1.11.1.21] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5whq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5whq OCA], [http://pdbe.org/5whq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5whq RCSB], [http://www.ebi.ac.uk/pdbsum/5whq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5whq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KATG_NEUCR KATG_NEUCR]] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. | + | [https://www.uniprot.org/uniprot/KATG_NEUCR KATG_NEUCR] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Catalase|Catalase]] | + | *[[Catalase 3D structures|Catalase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Catalase peroxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Neucr]] | + | [[Category: Neurospora crassa OR74A]] |
| - | [[Category: Diaz-Vilchis, A]] | + | [[Category: Diaz-Vilchis A]] |
| - | [[Category: Hansberg, W]] | + | [[Category: Hansberg W]] |
| - | [[Category: Rudino-Pinera, E]] | + | [[Category: Rudino-Pinera E]] |
| - | [[Category: Vega-Garcia, V]] | + | [[Category: Vega-Garcia V]] |
| - | [[Category: Catalase-peroxidase]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Hydrogen peroxide]]
| + | |
| - | [[Category: Neurospora crassa]]
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| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
KATG_NEUCR Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Publication Abstract from PubMed
CAT-2, a cytosolic catalase-peroxidase (CP) from Neurospora crassa, which is induced during asexual spore formation, was heterologously expressed and characterized. CAT-2 had the Met-Tyr-Trp (M-Y-W) adduct required for catalase activity. Its KM for H2O2 was micromolar for peroxidase and millimolar for catalase activity. A Em = -158 mV reduction potential value was obtained and the Soret band shift suggested a mixture of low and high spin ferric iron. CAT-2 EPR spectrum at 10 K indicated an axial and a rhombic component. With peroxyacetic acid (PAA), formation of Compound I* was observed with EPR. CAT-2 homodimer crystallographic structure contained two K(+) ions; Glu107 residues were displaced to bind them. CAT-2 showed the essential amino acid residues for activity in similar positions to other CPs. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 was oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other N. crassa enzymes that utilize H2O2 as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to H2O2 selection in water.
Structure, kinetics, molecular and redox properties of a cytosolic and developmentally regulated fungal catalase-peroxidase.,Vega-Garcia V, Diaz-Vilchis A, Saucedo-Vazquez JP, Solano-Peralta A, Rudino-Pinera E, Hansberg W Arch Biochem Biophys. 2018 Jan 2;640:17-26. doi: 10.1016/j.abb.2017.12.021. PMID:29305053[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vega-Garcia V, Diaz-Vilchis A, Saucedo-Vazquez JP, Solano-Peralta A, Rudino-Pinera E, Hansberg W. Structure, kinetics, molecular and redox properties of a cytosolic and developmentally regulated fungal catalase-peroxidase. Arch Biochem Biophys. 2018 Jan 2;640:17-26. doi: 10.1016/j.abb.2017.12.021. PMID:29305053 doi:http://dx.doi.org/10.1016/j.abb.2017.12.021
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