Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/15322
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dc.contributor.authorMaralihalli, Gururaj B-
dc.contributor.authorBhagwat, Anil S-
dc.date.accessioned2012-12-25T18:48:44Z-
dc.date.available2012-12-25T18:48:44Z-
dc.date.issued2001-12-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/15322-
dc.description361-367en_US
dc.description.abstractMaize phosphoenolpyruvate carboxylase (PEPC) was rapidly and completely inactivated by very low concentrations of trypsin at 37°C. PEP+Mg2+ and several other effectors of PEP carboxylase offered substantial protection against trypsin inactivation. Inactivation resulted from a fairly specific cleavage of 20 kDa peptide from the enzyme subunit. Limited proteolysis under catalytic condition (in presence of PEP, Mg2+ and HCO3) although yielded a truncated subunit of 90 kDa, did not affect the catalytic function appreciably but desensitized the enzyme to the effectors like glucose-6-phosphate glycine and malate. However, under non-catalytic condition, only malate sensitivity was appreciably affected. Significant protection of the enzyme activity against trypsin during catalytic phase could be either due to a conformational change induced on substrate binding. Several lines of evidence indicate that the inactivation caused by a cleavage at a highly conserved C-terminal end of the subunit.en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.38(6) [December 2001]en_US
dc.titleLimited proteolysis by trypsin influences activity of maize phosphoenolpyruvate carboxylaseen_US
dc.typeArticleen_US
Appears in Collections:IJBB Vol.38(6) [December 2001]

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