Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/15322
Title: Limited proteolysis by trypsin influences activity of maize phosphoenolpyruvate carboxylase
Authors: Maralihalli, Gururaj B
Bhagwat, Anil S
Issue Date: Dec-2001
Publisher: NISCAIR-CSIR, India
Abstract: Maize 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.
Page(s): 361-367
URI: http://hdl.handle.net/123456789/15322
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.38(6) [December 2001]

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