ATP:citrate lyase of Rhodotorula gracilis: purification and properties.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
View Archive Info| Field | Value | |
| Relation |
http://ir.cftri.com/2351/
BBA-03-90 |
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| Title |
ATP:citrate lyase of Rhodotorula gracilis: purification and properties.
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| Creator |
Shashi, K.
Bachhawat, A. K. Joseph, R. |
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| Subject |
05 Enzymes
19 Yeast |
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| Description |
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.
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| Date |
1990
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Language |
en
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| Identifier |
http://ir.cftri.com/2351/1/Kaithamana_Shashi%2C_Anand_K._Bachhawat%2C_Richard_Joseph.pdf
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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