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dc.contributor.authorKUMAR, SVSen_US
dc.contributor.authorPHALE, PSen_US
dc.contributor.authorDURANI, Sen_US
dc.contributor.authorWANGIKAR, PPen_US
dc.date.accessioned2011-08-04T11:58:59Zen_US
dc.date.accessioned2011-12-26T12:54:42Zen_US
dc.date.accessioned2011-12-27T05:42:54Z
dc.date.available2011-08-04T11:58:59Zen_US
dc.date.available2011-12-26T12:54:42Zen_US
dc.date.available2011-12-27T05:42:54Z
dc.date.issued2003en_US
dc.identifier.citationBIOTECHNOLOGY AND BIOENGINEERING, 83(4), 386-394en_US
dc.identifier.issn0006-3592en_US
dc.identifier.urihttp://dx.doi.org/10.1002/bit.10681en_US
dc.identifier.urihttp://dspace.library.iitb.ac.in/xmlui/handle/10054/9351en_US
dc.identifier.urihttp://hdl.handle.net/10054/9351
dc.description.abstractPlant and fungal laccases belong to the family of multi-copper oxidases and show much broader substrate specificity than other members of the family. Laccases have consequently been of interest for potential industrial applications. We have analyzed the essential sequence features of fungal laccases based on multiple sequence alignments of more than 100 laccases. This has resulted in identification of a set of four ungapped sequence regions, L1-L4, as the overall signature sequences that can be used to identify the laccases, distinguishing them within the broader class of multi-copper oxidases. The 12 amino acid residues in the enzymes serving as the copper ligands are housed within these four identified conserved regions, of which L2 and L4 conform to the earlier reported copper signature sequences of multi-copper oxidases while L1 and L3 are distinctive to the laccases. The mapping of regions L1-L4 on to the three-dimensional structure of the Coprinus cinerius laccase indicates that many of the non-copper-ligating residues of the conserved regions could be critical in maintaining a specific, more or less C-2 symmetric, protein conformational motif characterizing the active site apparatus of the enzymes. The observed intraprotein homologies between L1 and L3 and between L2 and L4 at both the structure and the sequence levels suggest that the quasi C-2 symmetric active site conformational motif may have arisen from a structural duplication event that neither the sequence homology analysis nor the structure homology analysis alone would have unraveled. Although the sequence and structure homology is not detectable in the rest of the protein, the relative orientation of region L1 with L2 is similar to that of L3 with L4. The structure duplication of first-shell and second-shell residues has become cryptic because the intraprotein sequence homology noticeable for a given laccase becomes significant only after comparing the conservation pattern in several fungal laccases. The identified motifs, L1-L4, can be useful in searching the newly sequenced genomes for putative laccase enzymes. (C) 2003 .en_US
dc.language.isoenen_US
dc.publisherJOHN WILEY & SONS INCen_US
dc.subjectWhite-Rot Fungusen_US
dc.subjectAspergillus-Nidulansen_US
dc.subjectCoprinus-Cinereusen_US
dc.subjectAngstrom Resolutionen_US
dc.subjectMolecular-Cloningen_US
dc.subjectTrametes-Villosaen_US
dc.subjectGeneen_US
dc.subjectExpressionen_US
dc.subjectPurificationen_US
dc.subjectMatricesen_US
dc.subject.otherLaccasesen_US
dc.subject.otherMulti-Copper Oxidasesen_US
dc.subject.otherCopper Signature Sequenceen_US
dc.subject.otherMultiple Sequence Alignmenten_US
dc.subject.otherStructure Alignmenten_US
dc.subject.otherGene Duplicationen_US
dc.titleCombined sequence and structure analysis of the fungal laccase familyen_US
dc.typeArticleen_US


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