In Vitro Alterations of L-asparaginase Activity of Tetrahymena Pyriformis by Lipids

Overview

Journal Mol Cell Biochem

Publisher Springer

Specialty Biochemistry

Date 1988 Oct 1

PMID 3143910

Citations 3

Authors

S A Tsirka

D A Kyriakidis

Affiliations

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Abstract

A membrane-bound L-asparaginase (EC 3.5.1.1) of Tetrahymena pyriformis was purified to homogeneity. The purified enzyme is a lipoprotein, since it is inactivated by phospholipase C and its activity is restored by the addition of naturally occurring lipids, such as phosphatidylcholine, triolein and oleyl acetate. The relative effectiveness of a variety of phospholipids, free saturated and unsaturated fatty acids, or neutral lipids, such as esters of fatty acids and glycerides, with respect to the activation of purified L-asparaginase is compared. Enzyme activity is reconstituted in the presence of lipids and evidence for the formation of an enzyme-phospholipid complex is presented. The data of this report suggest that L-asparaginase may have a requirement for lipids that reconstitute a physiological hydrophobic environment, similar to the one existing in vivo.

Citing Articles

L-asparaginase of Thermus thermophilus: purification, properties and identification of essential amino acids for its catalytic activity.

Pritsa A, Kyriakidis D Mol Cell Biochem. 2001; 216(1-2):93-101.

PMID: 11216870 DOI: 10.1023/a:1011066129771.

Antiproliferative activity of L-asparaginase of Tetrahymena pyriformis on human breast cancer cell lines.

Kyriakidis D, Tsirka S, Tsavdaridis I, Iliadis S, Kortsaris A Mol Cell Biochem. 1990; 96(2):137-42.

PMID: 2125695 DOI: 10.1007/BF00420905.

L-asparaginase of Tetrahymena pyriformis is associated with a kinase activity.

Tsirka S, Kyriakidis D Mol Cell Biochem. 1990; 95(1):77-87.

PMID: 2114526 DOI: 10.1007/BF00219533.

References

Claassen E, van Rooijen N . A comparative study on the effectiveness of various procedures for attachment of two proteins (L-asparaginase and horse radish peroxidase) to the surface of liposomes. Prep Biochem. 1983; 13(2):167-74. DOI: 10.1080/00327488308068746. View

Fishman Y, CITRI N . L-asparaginase entrapped in liposomes: preparation and properties. FEBS Lett. 1975; 60(1):17-20. DOI: 10.1016/0014-5793(75)80408-x. View

Paul J, Cooksey K . Regulation of asparaginase, glutamine synthetase, and glutamate dehydrogenase in response to medium nitrogen concentrations in a euryhaline chlamydomonas species. Plant Physiol. 1981; 68(6):1364-8. PMC: 426104. DOI: 10.1104/pp.68.6.1364. View

Ho P, Milikin E, Bobbitt J, GRINNAN E, Burck P, Frank B . Crystalline L-asparaginase from Escherichia coli B. I. Purification and chemical characterization. J Biol Chem. 1970; 245(14):3708-15. View

Roon R, Murdoch M, Kunze B, Dunlop P . Derepression of asparaginase II during exponential growth of Saccharomyces cerevisiae on ammonium ion. Arch Biochem Biophys. 1982; 219(1):101-9. DOI: 10.1016/0003-9861(82)90138-2. View

Khan A, Pal S, Raghavan S, Bhattacharyya P . Studies on Serratia marcescens L-asparaginase. Biochem Biophys Res Commun. 1970; 41(3):525-33. DOI: 10.1016/0006-291x(70)90044-6. View

Jensen J, Schutzbach J . Activation of dolichyl-phospho-mannose synthase by phospholipids. Eur J Biochem. 1985; 153(1):41-8. DOI: 10.1111/j.1432-1033.1985.tb09264.x. View

Coleman R . Membrane-bound enzymes and membrane ultrastructure. Biochim Biophys Acta. 1973; 300(1):1-30. DOI: 10.1016/0304-4157(73)90010-5. View

Svobodova O . Induction of L-asparaginase synthesis in Escherichia coli. Biochim Biophys Acta. 1973; 321(2):643-52. DOI: 10.1016/0005-2744(73)90208-8. View

10.

JEREBZOFF-QUINTIN S, Jerebzoff S . Reversible self-phosphorylation of asparaginase complex in Leptosphaeria michotii: characterization of associated protein kinase and protein phosphatase activities. Biochem Biophys Res Commun. 1986; 140(3):1135-42. DOI: 10.1016/0006-291x(86)90753-9. View

11.

Netrval J . Stimulation of L-asparaginase production in Escherichia coli by organic and amino acids. Folia Microbiol (Praha). 1977; 22(2):106-16. DOI: 10.1007/BF02881635. View

12.

Erlanson-Albertsson C . The interaction between pancreatic lipase and colipase: a protein-protein interaction regulated by a lipid. FEBS Lett. 1983; 162(2):225-9. DOI: 10.1016/0014-5793(83)80760-1. View

13.

Kamerud J, Roon R . Asparaginase II of Saccharomyces cerevisiae: selection of four mutations that cause derepressed enzyme synthesis. J Bacteriol. 1986; 165(1):293-6. PMC: 214403. DOI: 10.1128/jb.165.1.293-296.1986. View

14.

WRISTON Jr J . Asparaginase. Methods Enzymol. 1985; 113:608-18. DOI: 10.1016/s0076-6879(85)13082-x. View

15.

BEAUFAY H, DE DUVE C . [The hexosephosphatase system. VI. Attempted fractionation of microsomes containing glucose-6-phosphatase]. Bull Soc Chim Biol (Paris). 1954; 36(11-12):1551-68. View

16.

Martinek K, Levashov A, Klyachko N, Khmelnitski Y, Berezin I . Micellar enzymology. Eur J Biochem. 1986; 155(3):453-68. DOI: 10.1111/j.1432-1033.1986.tb09512.x. View

17.

Jarrett H . Response of three enzymes to oleic acid, trypsin, and calmodulin chemically modified with a reactive phenothiazine. J Biol Chem. 1986; 261(11):4967-72. View

18.

Duttera S, Byrne W, Ganoza M . Studies on the phospholipid requirement of glucose 6-phosphatase. J Biol Chem. 1968; 243(9):2216-28. View

19.

Ernster L, Siekevitz P, Palade G . ENZYME-STRUCTURE RELATIONSHIPS IN THE ENDOPLASMIC RETICULUM OF RAT LIVER : A Morphological and Biochemical Study. J Cell Biol. 2009; 15(3):541-62. PMC: 2106166. DOI: 10.1083/jcb.15.3.541. View

20.

Dyatlovitskaya E, Lemenovskaya A, BERGELSON L . Use of protein-mediated lipid exchange in the study of membrane-bound enzymes. The lipid dependence of glucose-6-phosphatase. Eur J Biochem. 1979; 99(3):605-12. DOI: 10.1111/j.1432-1033.1979.tb13293.x. View