Effect of arginine modifying reagents on pigeon liver fatty acids synthetase: Evidence for the presence of essential arginine residues at the β-ketoacyl reductase and enoyl -CoA reductase domain

Mukherjee, Sanchita; Kaliyar, Sarvagya S

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Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/15378

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DC Field	Value	Language
dc.contributor.author	Mukherjee, Sanchita	-
dc.contributor.author	Kaliyar, Sarvagya S	-
dc.date.accessioned	2012-12-28T11:36:15Z	-
dc.date.available	2012-12-28T11:36:15Z	-
dc.date.issued	2000-02	-
dc.identifier.issn	0975-0959 (Online); 0301-1208 (Print)	-
dc.identifier.uri	http://hdl.handle.net/123456789/15378	-
dc.description	28-33	en_US
dc.description.abstract	Pigeon liver fatty acid synthetase was inactivated by arginine modifying reagent, phenylglyoxal and 2,3 -butanedione. The inactivation of overall fatty acid synthetase was accompanied by the loss of β-ketoacyl reductase and enoyl-CoA reductase activity. The inactivation followed a pseudo-first order kinetics and sum of the second order rate constants for the two reductase reactions equaled that for the synthetase reaction. Inactivation of all three activities was prevented by NADPH or its analogs 2',5'-ADP and 2'-AMP but not by the corresponding nucleotides containing the 5'- phosphate. These results suggest that binding of NADPH to fatty acid synthetase involves specific interaction of the 2'-phosphate with the guanidine group of arginine residues at the active site of the two reductases, pH - Dependent inactivation by phenylglyoxal indicated that a group with a pk_a 7.5 is involved in the loss of enzyme activity. Stoichiometric results showed that 4 out of 164 arginine residues per enzyme molecule were essential for the enzyme activity.	en_US
dc.language.iso	en_US	en_US
dc.publisher	NISCAIR-CSIR, India	en_US
dc.rights	CC Attribution-Noncommercial-No Derivative Works 2.5 India	en_US
dc.source	IJBB Vol.37(1) [February 2000]	en_US
dc.title	Effect of arginine modifying reagents on pigeon liver fatty acids synthetase: Evidence for the presence of essential arginine residues at the β-ketoacyl reductase and enoyl -CoA reductase domain	en_US
dc.type	Article	en_US
Appears in Collections:	IJBB Vol.37(1) [February 2000]

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