1sch
From Proteopedia
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==Overview== | ==Overview== | ||
| - | BACKGROUND. Peroxidases catalyze a wide variety of peroxide-dependent, oxidations. Based on sequence alignments, heme peroxidases have been, divided into three classes. Crystal structures are available for, peroxidases of classes I and II, but until now no structure has been, determined for class III, the classical extracellular plant peroxidases., RESULTS. The crystal structure of peanut peroxidase has been solved to 2.7, A resolution. The helical fold is similar to that of known peroxidase, structures. The 294-residue polypeptide chain is accompanied by a heme and, two calcium ions, and there is some evidence of glycosylation., CONCLUSIONS. This is the first complete structure of a class III, peroxidase and as such should serve as a model for other class III enzymes, including the ... | + | BACKGROUND. Peroxidases catalyze a wide variety of peroxide-dependent, oxidations. Based on sequence alignments, heme peroxidases have been, divided into three classes. Crystal structures are available for, peroxidases of classes I and II, but until now no structure has been, determined for class III, the classical extracellular plant peroxidases., RESULTS. The crystal structure of peanut peroxidase has been solved to 2.7, A resolution. The helical fold is similar to that of known peroxidase, structures. The 294-residue polypeptide chain is accompanied by a heme and, two calcium ions, and there is some evidence of glycosylation., CONCLUSIONS. This is the first complete structure of a class III, peroxidase and as such should serve as a model for other class III enzymes, including the much-studied horseradish peroxidase. It may also aid in the, interpretation of functional differences between the peroxidase classes., Ten helices conserved in class I and II peroxidases are also found in, peanut peroxidase. Key residues of the heme environment and the location, of two calcium ions are shared with class II peroxidases. Peanut, peroxidase contains three unique helices, two of which contribute to the, substrate access channel leading to the heme edge. |
==About this Structure== | ==About this Structure== | ||
| - | 1SCH is a | + | 1SCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea] with NAG, CA and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Structure known Active Sites: ADC, ADH, APC, APH, BDC, BDH, BPC and BPH. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SCH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:00:04 2007'' |
Revision as of 10:54, 5 November 2007
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PEANUT PEROXIDASE
Overview
BACKGROUND. Peroxidases catalyze a wide variety of peroxide-dependent, oxidations. Based on sequence alignments, heme peroxidases have been, divided into three classes. Crystal structures are available for, peroxidases of classes I and II, but until now no structure has been, determined for class III, the classical extracellular plant peroxidases., RESULTS. The crystal structure of peanut peroxidase has been solved to 2.7, A resolution. The helical fold is similar to that of known peroxidase, structures. The 294-residue polypeptide chain is accompanied by a heme and, two calcium ions, and there is some evidence of glycosylation., CONCLUSIONS. This is the first complete structure of a class III, peroxidase and as such should serve as a model for other class III enzymes, including the much-studied horseradish peroxidase. It may also aid in the, interpretation of functional differences between the peroxidase classes., Ten helices conserved in class I and II peroxidases are also found in, peanut peroxidase. Key residues of the heme environment and the location, of two calcium ions are shared with class II peroxidases. Peanut, peroxidase contains three unique helices, two of which contribute to the, substrate access channel leading to the heme edge.
About this Structure
1SCH is a Single protein structure of sequence from Arachis hypogaea with NAG, CA and HEM as ligands. Active as Peroxidase, with EC number 1.11.1.7 Structure known Active Sites: ADC, ADH, APC, APH, BDC, BDH, BPC and BPH. Full crystallographic information is available from OCA.
Reference
The crystal structure of peanut peroxidase., Schuller DJ, Ban N, Huystee RB, McPherson A, Poulos TL, Structure. 1996 Mar 15;4(3):311-21. PMID:8805539
Page seeded by OCA on Mon Nov 5 13:00:04 2007
Categories: Arachis hypogaea | Peroxidase | Single protein | Poulos, T.L. | Schuller, D.J. | CA | HEM | NAG | Calcium binding | Glycosylation | Oxidoreductase
