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ATP:citrate lyase of Rhodotorula gracilis: purification and properties.

Shashi, K. and Bachhawat, A. K. and Joseph, R. (1990) ATP:citrate lyase of Rhodotorula gracilis: purification and properties. Biochimica et Biophysica Acta, 1033 (1). pp. 23-30. ISSN 0006-3002

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ATP:citrate lyase was purified from the oleaginous yeast Rhodotorula gracilis to homogeneity as judged by polyacrylamide gel electrophoresis, using a novel citrate-Sepharose procedure. The enzyme was found to have a molecular weight of 520,000 and consisted of four identical subunits (Mr = 120,000). Two minor low molecular weight bands were observed on SDS-PAGE (Mr 51,000 and 49,000). Trypsin digestion experiments indicated that these could have been the result of limited proteolysis by an endogenous trypsin-like proteinase. In this respect, it resembles the mammalian ATP:citrate lyase. The enzyme was stimulated by NH+4 ions and inhibited by palmitoyl, lauroyl, oleoyl, myristoyl and stearoyl-CoA esters, glutamate and glucose 6-phosphate but not by acetyl-CoA or shorter chain fatty acyl-CoA esters. The enzyme exhibited normal Michaelis-Menten kinetics for citrate; however there was a 3-fold increase in Km with a high concentration of Cl- ions (0.25 M). The possible regulatory roles of ATP:citrate lyase in R. gracilis are discussed in the light of these findings.

Item Type: Article
Uncontrolled Keywords: ATP:citrate lyase, microorganism,
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 19 Yeast
Divisions: Food Microbiology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 09 Mar 2011 07:06
Last Modified: 01 Oct 2018 09:36
URI: http://ir.cftri.com/id/eprint/2351

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