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4qom

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Revision as of 18:34, 1 February 2017

Bacillus pumilus catalase with pyrogallol bound

Structural highlights

4qom is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	4qol, 4qon, 4qoo, 4qop, 4qoq, 4qor
Activity:	Catalase, with EC number 1.11.1.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Heme-containing catalases and catalase-peroxidases catalyze the dismutation of hydrogen peroxide as their predominant catalytic activity, but in addition, individual enzymes support low levels of peroxidase and oxidase activities, produce superoxide and activate isoniazid as an anti-tubercular drug. The recent report of a heme enzyme with catalase, peroxidase and penicillin oxidase activities in Bacillus pumilus and its categorization as an unusual catalase-peroxidase led us to investigate the enzyme for comparison with other catalase-peroxidases, catalases and peroxidases. Characterization revealed a typical homotetrameric catalase with one pentacoordinated heme b per subunit (Tyr340 being the axial ligand), albeit in two orientations, and a very fast catalatic turnover rate (kcat = 339,000s-1 ). In addition, the enzyme supported a much slower (kcat approximately 20s-1 ) peroxidatic activity utilizing substrates as diverse as ABTS and polyphenols, but no oxidase activity. Two binding sites, one in the main access channel and the other on the protein surface, accommodating pyrogallol, catechol, resorcinol, guaiacol, hydroquinone and 2-chlorophenol were identified in crystal structures at 1.65-1.95 A. A third site, in the heme distal side, accommodating only pyrogallol and catechol, interacting with the heme iron and the catalytic His and Arg residues, was also identified. This site was confirmed in solution by EPR spectroscopy, which also showed that the phenolic oxygen was not directly coordinated to the heme iron (no low-spin conversion of the heme FeIII high-spin EPR signal upon substrate binding). This is the first demonstration of phenolic substrates directly accessing the heme distal side of a catalase. This article is protected by copyright. All rights reserved.

Unprecedented access of phenolic substrates to the heme active site of a catalase: Substrate binding and peroxidase-like reactivity of Bacillus pumilus catalase monitored by X-ray crystallography and EPR spectroscopy.,Loewen PC, Villanueva J, Switala J, Donald LJ, Ivancich A Proteins. 2015 Feb 7. doi: 10.1002/prot.24777. PMID:25663126^[1]

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

References

↑ Loewen PC, Villanueva J, Switala J, Donald LJ, Ivancich A. Unprecedented access of phenolic substrates to the heme active site of a catalase: Substrate binding and peroxidase-like reactivity of Bacillus pumilus catalase monitored by X-ray crystallography and EPR spectroscopy. Proteins. 2015 Feb 7. doi: 10.1002/prot.24777. PMID:25663126 doi:http://dx.doi.org/10.1002/prot.24777

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4qom"

Categories: Catalase | Loewen, P C | Catalase and peroxidase | Catalase fold | Oxidoreductase

@@ Line 1: / Line 1: @@
 ==Bacillus pumilus catalase with pyrogallol bound==
 <StructureSection load='4qom' size='340' side='right' caption='[[4qom]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qol|4qol]], [[4qon|4qon]], [[4qoo|4qoo]], [[4qop|4qop]], [[4qoq|4qoq]], [[4qor|4qor]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </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=4qom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qom OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qom RCSB], [http://www.ebi.ac.uk/pdbsum/4qom PDBsum]</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=4qom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qom OCA], [http://pdbe.org/4qom PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qom RCSB], [http://www.ebi.ac.uk/pdbsum/4qom PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qom ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4qom" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Catalase|Catalase]]
 == References ==
 <references/>

4qom

From Proteopedia

Revision as of 18:34, 1 February 2017

Bacillus pumilus catalase with pyrogallol bound

Structural highlights

Publication Abstract from PubMed

References

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