Aspartokinase of Lemna Paucicostata Hegelm. 6746

Overview

Journal Plant Physiol

Specialty Physiology

Date 1989 Aug 1

PMID 16666968

Citations 7

Authors

J Giovanelli

S H Mudd

A H Datko

Affiliations

Soon will be listed here.

Abstract

A sensitive and specific method was developed for assay of aspartokinase (EC 2.7.2.4) in crude extracts of Lemna paucicostata. Lysine inhibited approximately 93%, and threonine approximately 6%; together, these amino acids inhibited 99%. Inhibition by lysine was synergistically increased by S-adenosylmethionine, which by itself had no effect on activity. Essentially complete inhibition of threonine-resistant activity was obtained with lysine, and of lysine-resistant activity with threonine. Inhibition by lysine and threonine was additive, with no indication of concerted inhibition. Aspartate concentration had no effect on the relative proportions of lysine- and threonine-sensitive activities. Aspartokinase activity was in large excess of that reported by other workers, the maximum capacity (V(max)) far exceeding the in vivo requirements. Estimations of rates of aspartokinase in vivo suggest that the step catalyzed by this enzyme may not be the overall ;rate-limiting' one for entry of 4-carbon units into the aspartate family of amino acids, and that feedback inhibition of this enzyme by lysine and threonine may not be a major factor in regulating flux through this step.

Citing Articles

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Genetic and amino-acid analysis of two maize threonine-overproducing, lysine-insensitive aspartate kinase mutants.

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Kinetic studies of lysine-sensitive aspartate kinase purified from maize suspension cultures.

Dotson S, Somers D, Gengenbach B Plant Physiol. 1990; 93(1):98-104.

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References

Datko A, Mudd S . Methionine biosynthesis in lemna: inhibitor studies. Plant Physiol. 1982; 69(5):1070-6. PMC: 426361. DOI: 10.1104/pp.69.5.1070. View

Giovanelli J, Mudd S, Datko A . In vivo regulation of de novo methionine biosynthesis in a higher plant (lemna). Plant Physiol. 1985; 77(2):450-5. PMC: 1064534. DOI: 10.1104/pp.77.2.450. View

Shames S, Ash D, Wedler F, Villafranca J . Interaction of aspartate and aspartate-derived antimetabolites with the enzymes of the threonine biosynthetic pathway of Escherichia coli. J Biol Chem. 1984; 259(24):15331-9. View

Zivin J, WAUD D . How to analyze binding, enzyme and uptake data: the simplest case, a single phase. Life Sci. 1982; 30(17):1407-22. DOI: 10.1016/0024-3205(82)90554-9. View

Datko A, Mudd S, Giovanelli J . Lemna paucicostata Hegelm. 6746: DEVELOPMENT OF STANDARDIZED GROWTH CONDITIONS SUITABLE FOR BIOCHEMICAL EXPERIMENTATION. Plant Physiol. 1980; 65(5):906-12. PMC: 440448. DOI: 10.1104/pp.65.5.906. View

Giovanelli J, Mudd S, Datko A . Regulatory Structure of the Biosynthetic Pathway for the Aspartate Family of Amino Acids in Lemna paucicostata Hegelm. 6746, with Special Reference to the Role of Aspartokinase. Plant Physiol. 1989; 90(4):1584-99. PMC: 1061929. DOI: 10.1104/pp.90.4.1584. View

Wong K, Dennis D . Aspartokinase in Lemna minor L: Studies on the in Vivo and in Vitro Regulation of the Enzyme. Plant Physiol. 1973; 51(2):327-31. PMC: 366259. DOI: 10.1104/pp.51.2.327. View

Rognes S, Lea P, Miflin B . S-adenosylmethionine--a novel regulator of aspartate kinase. Nature. 1980; 287(5780):357-9. DOI: 10.1038/287357a0. View

Thompson G, Datko A, Mudd S, Giovanelli J . Methionine Biosynthesis in Lemna: STUDIES ON THE REGULATION OF CYSTATHIONINE gamma-SYNTHASE, O-PHOSPHOHOMOSERINE SULFHYDRYLASE, AND O-ACETYLSERINE SULFHYDRYLASE. Plant Physiol. 1982; 69(5):1077-83. PMC: 426362. DOI: 10.1104/pp.69.5.1077. View

10.

Giovanelli J, Mudd S, Datko A, Thompson G . Effects of Orthophosphate and Adenosine 5'-Phosphate on Threonine Synthase and Cystathionine gamma-Synthate of Lemna paucicostata Hegelm. 6746. Plant Physiol. 1986; 81(2):577-83. PMC: 1075379. DOI: 10.1104/pp.81.2.577. View

11.

Datta P, Prakash L . Aspartokinase of Rhodopseudomonas spheroides. Regulation of enzyme activity by aspartate beta-semialdehyde. J Biol Chem. 1966; 241(24):5827-35. View

12.

Giovanelli J, Mudd S, Datko A . In Vivo Regulation of Threonine and Isoleucine Biosynthesis in Lemna paucicostata Hegelm. 6746. Plant Physiol. 1988; 86(2):369-77. PMC: 1054491. DOI: 10.1104/pp.86.2.369. View

13.

Lea P, Mills W, Miflin B . The isolation of a lysine-sensitive aspartate kinase from pea leaves and its involvement in homoserine biosynthesis in isolated chloroplasts. FEBS Lett. 1979; 98(1):165-8. DOI: 10.1016/0014-5793(79)80175-1. View

14.

Mills W, Henke R, Burdge E, Wilson K . Intracellular localization of beta-aspartate kinase in spinach (Spinacea oleracea). FEBS Lett. 1979; 104(2):303-8. DOI: 10.1016/0014-5793(79)80839-x. View

15.

Datko A, Mudd S . Responses of Sulfur-Containing Compounds in Lemna paucicostata Hegelm. 6746 to Changes in Availability of Sulfur Sources. Plant Physiol. 1984; 75(2):474-9. PMC: 1066932. DOI: 10.1104/pp.75.2.474. View

16.

Newsholme E, Crabtree B . Theoretical principles in the approaches to control of metabolic pathways and their application to glycolysis in muscle. J Mol Cell Cardiol. 1979; 11(9):839-56. DOI: 10.1016/0022-2828(79)90480-2. View

17.

Chapman D, Leech R . Changes in Pool Sizes of Free Amino Acids and Amides in Leaves and Plastids of Zea mays during Leaf Development. Plant Physiol. 1979; 63(3):567-72. PMC: 542871. DOI: 10.1104/pp.63.3.567. View

18.

Bright S, Leggatt M, Miflin B . Amino Acid levels in carrot cell suspension culture: no correlation with aspartate kinase isoenzyme levels. Plant Physiol. 1979; 63(3):586-8. PMC: 542875. DOI: 10.1104/pp.63.3.586. View

19.

Shewry P, Miflin B . Properties and Regulation of Aspartate Kinase from Barley Seedlings (Hordeum vulgare L.). Plant Physiol. 1977; 59(1):69-73. PMC: 542332. DOI: 10.1104/pp.59.1.69. View

20.

Wong K, Dennis D . Aspartokinase from wheat germ: isolation, characterization, and regulation. Plant Physiol. 1973; 51(2):322-6. PMC: 366258. DOI: 10.1104/pp.51.2.322. View