Record Details


Field	Value

Title	Limited proteolysis by trypsin influences activity of maize phosphoenolpyruvate carboxylase

Creator	Maralihalli, Gururaj B Bhagwat, Anil S

Description	361-367 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.

Date	2012-12-25T18:48:44Z 2012-12-25T18:48:44Z 2001-12

Type	Article

Identifier	0975-0959 (Online); 0301-1208 (Print) http://hdl.handle.net/123456789/15322

Language	en_US

Rights	CC Attribution-Noncommercial-No Derivative Works 2.5 India

Publisher	NISCAIR-CSIR, India

Source	IJBB Vol.38(6) [December 2001]

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