Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/5573
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dc.contributor.authorPalanivelu, P-
dc.date.accessioned2009-07-27T03:47:31Z-
dc.date.available2009-07-27T03:47:31Z-
dc.date.issued2006-04-
dc.identifier.issn0975-0967 (Online); 0972-5849 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/5573-
dc.description148-162en_US
dc.description.abstractPolygalacturonases from various sources have been analyzed by ClustalW and T-COFFEE, for identification of conserved and functional motifs in them. All the 104 polygalacturonases analyzed by the above programs, revealed four highly conserved motifs, viz., NTD, G/QDD, G/SHG and RIK among them. Distance conservation between the motifs was also observed. Based on the available evidences from chemical modification studies on active site amino acids, site-directed mutagenesis, protein sequence analysis and X-ray crystallographic data, a mechanism of action is proposed for this group of enzymes.en_US
dc.language.isoen_USen_US
dc.publisherCSIRen_US
dc.relation.ispartofseriesInt. Cl.8 C12N9/38, 9/40en_US
dc.sourceIJBT Vol.5(2) [April 2006]en_US
dc.subjectpolygalacturonasesen_US
dc.subjectprotein sequence analysisen_US
dc.subjectactive site amino acidsen_US
dc.subjectdistance conservation between motifsen_US
dc.subjectmechanism of actionen_US
dc.titlePolygalacturonases: Active site analyses and mechanism of actionen_US
dc.typeArticleen_US
Appears in Collections:IJBT Vol.05(2) [April 2006]

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