tailieunhanh - Báo cáo khoa học: Functional role of fumarate site Glu59 involved in allosteric regulation and subunit–subunit interaction of human mitochondrial NAD(P)+-dependent malic enzyme

The two main mammalian calpains, 1 and 2, are heterodimers of a large 80 kDa and a small 28 kDa subunit that together bind multiple calcium ions during enzyme activation. The main contact between the two subunits of these intracellular cysteine proteases is through a pairing of the fifth EF-hand of their C-terminal penta-EF-hand (PEF) domains. | ỊFEBS Journal Functional role of fumarate site Glu59 involved in allosteric regulation and subunit-subunit interaction of human mitochondrial NAD P -dependent malic enzyme Ju-Yi Hsieh1 Yu-Hsiu Chiang1 Kuan-Yu Chang1 and Hui-Chih Hung1 2 1 Department of Life Sciences NationalChung-Hsing University Taichung Taiwan 2 Institute of Bioinformatics NationalChung-Hsing University Taichung Taiwan Keywords allosteric regulation analytical ultracentrifugation electrostatic interaction malic enzyme mutagenesis Correspondence . Hung Department of Life Sciences and Institute of Bioinformatics National Chung-Hsing University 250 Kuo-Kuang Road Taichung 40227 Taiwan Fax 886 4 22851856 Tel 886 4 22840416 ext. 615 E-mail hchung@ These authors contributed equally to this work Received 30 July 2008 revised 19 November 2008 accepted 4 December 2008 doi Here we report on the role of Glu59 in the fumarate-mediated allosteric regulation of the human mitochondrial NAD P -dependent malic enzyme m-NAD-ME . In the present study Glu59 was substituted by Asp Gln or Leu. Our kinetic data strongly indicated that the charge properties of this residue significantly affect the allosteric activation of the enzyme. The E59L enzyme shows nonallosteric kinetics and the E59Q enzyme displays a much higher threshold in enzyme activation with elevated activation constants KA Fum and aKA Fum. The E59D enzyme although retaining the allosteric property is quite different from the wild-type in enzyme activation. The KA Fum and aKA Fum of E59D are also much greater than those of the wild-type indicating that not only the negative charge of this residue but also the group specificity and side chain interactions are important for fumarate binding. Analytical ultracentrifugation analysis shows that both the wild-type and E59Q enzymes exist as a dimer-tetramer equilibrium. In contrast to the E59Q mutant the E59D mutant displays predominantly a dimer form .

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