Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/834
Full metadata record
DC FieldValueLanguage
dc.contributor.authorMehta, Gurkaran Singh-
dc.contributor.otherPandit, Shashi Bhushan-
dc.date.accessioned2017-07-18T07:27:28Z-
dc.date.available2017-07-18T07:27:28Z-
dc.date.issued2017-07-18-
dc.identifier.urihttp://hdl.handle.net/123456789/834-
dc.description.abstract4-α-Glucanotransferase, an enzyme from Pyrococcus furiosus, catalyzes the hydrolysis of a glucose unit from a donor molecule, and transfers it to an acceptor molecule. The sequence of this enzyme is very much similar to 4-α-Glucanotransferase from Thermococcus litoralis. The donor and acceptor molecules are carbohydrates of varying length. The donor and acceptor sites are present within the enzyme only. The donor site is present in domain-I having catalytic residues Glutamate-124 and Aspartate-215, working in a acid-base catalysis kind of mechanism, similar in case of the enzyme from Thermococcus litoralis. The acceptor site is present in domain-II having interacting residues Histidine-369 and Arginine-372. The function of domain-III is not yet known.en_US
dc.description.sponsorshipIISER-Men_US
dc.language.isoenen_US
dc.publisherIISER-Men_US
dc.subjectBiologyen_US
dc.subject4-α-Glucanotransferaseen_US
dc.subjectEnzymeen_US
dc.subjectPyrococcus furiosusen_US
dc.subjectThermococcus litoralisen_US
dc.titleStructural Analysis of 4-α-Glucanotransferase from Pyrococcus Furiosusen_US
dc.typeThesisen_US
dc.guideGuptasarma, P.-
Appears in Collections:MS Dissertation by MP-2014

Files in This Item:
File Description SizeFormat 
MP14001.pdf2.26 MBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.