In silico prediction and characterization of 3D structure and binding properties of catalase from the commercially important crab, Scylla serrata
The enzyme catalase breaks down H(2)O(2), a potentially harmful oxidant, to H(2)O and O(2). Besides oxidase activity, the enzyme also exhibits peroxidase activity. Therefore, it plays an important role in maintaining health and regulating pathophysiology of the organisms. However, 3D structure of this important enzyme in invertebrates particularly in crabs is not yet available. Therefore, an attempt has been made to predict the structure of the crab catalase and to envisage its catalytic interaction with H(2)O(2). A three dimensional model of crab catalase was constructed using the NADPH binding site on Beef Liver catalase from Bos taurus (PDBID: 7CAT) as template by comparative modeling approach. Backbone conformation of the modeled structure by PROCHECK revealed that more than 98% of the residues fell in the allowed regions, ERRAT results confirmed good quality of modeled structure and VERIFY3D profile was satisfying. Molecular docking has been used to know the binding modes of hydrogen peroxide with the crab catalase protein. The receptor structures used for docking were derived from molecular dynamics (MD) simulations of homology modeled structure. The docking results showed that the three important determinant residues Arg68, Val70 and Arg108 in catalase were binding with H(2)O(2) as they had strong hydrogen bonding contacts with the substrate. Our analysis provides insight into the structural properties of crab catalase and defines its active sites for binding with substrate. These data are important for further studies of catalase of invertebrates in general and that of crabs in particular.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2011 |
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Erschienen: |
2011 |
Enthalten in: |
Zur Gesamtaufnahme - volume:3 |
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Enthalten in: |
Interdisciplinary sciences, computational life sciences - 3(2011), 2 vom: 05. Juni, Seite 110-20 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Paital, Biswaranjan [VerfasserIn] |
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Links: |
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Themen: |
42VZT0U6YR |
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Anmerkungen: |
Date Completed 09.04.2012 Date Revised 19.05.2016 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1007/s12539-011-0071-z |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM207939136 |
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245 | 1 | 0 | |a In silico prediction and characterization of 3D structure and binding properties of catalase from the commercially important crab, Scylla serrata |
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520 | |a The enzyme catalase breaks down H(2)O(2), a potentially harmful oxidant, to H(2)O and O(2). Besides oxidase activity, the enzyme also exhibits peroxidase activity. Therefore, it plays an important role in maintaining health and regulating pathophysiology of the organisms. However, 3D structure of this important enzyme in invertebrates particularly in crabs is not yet available. Therefore, an attempt has been made to predict the structure of the crab catalase and to envisage its catalytic interaction with H(2)O(2). A three dimensional model of crab catalase was constructed using the NADPH binding site on Beef Liver catalase from Bos taurus (PDBID: 7CAT) as template by comparative modeling approach. Backbone conformation of the modeled structure by PROCHECK revealed that more than 98% of the residues fell in the allowed regions, ERRAT results confirmed good quality of modeled structure and VERIFY3D profile was satisfying. Molecular docking has been used to know the binding modes of hydrogen peroxide with the crab catalase protein. The receptor structures used for docking were derived from molecular dynamics (MD) simulations of homology modeled structure. The docking results showed that the three important determinant residues Arg68, Val70 and Arg108 in catalase were binding with H(2)O(2) as they had strong hydrogen bonding contacts with the substrate. Our analysis provides insight into the structural properties of crab catalase and defines its active sites for binding with substrate. These data are important for further studies of catalase of invertebrates in general and that of crabs in particular | ||
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