Aspartate Aminotransferases OfPanicum Miliaceum L. AndPanicum Antidotale Retz. : Inactivation and Reconstitution

Overview

Journal Planta

Specialty Biology

Date 2013 Nov 27

PMID 24276278

Authors

C Balkow

G F Wildner

Affiliations

Soon will be listed here.

Abstract

L-Aspartate: 2-oxoglutarate transaminase was isolated and partially purified from leaves ofPanicum miliaceum (C4, NAD-malic enzyme type) and ofPanicum antidotale (C4, NADP-malic enzyme type). In each preparation two isoenzymes with different kinetic properties could be characterized. The enzyme activity was irreversibly inhibited by 2-aminooxyacetic acid and by 2-amino-4-methoxy-3-butenoic acid. The first inhibitor reacted with pyridoxal 5-phosphate, and its inhibition could be reversed by the exchange of the modified coenzyme. The second inhibitor binds not only to the coenzyme pyridoxal 5-phosphate, but also to the apoprotein. The results of the dissociation and reconstitution experiments were in agreement with the kinetic data, showing that the mode of inactivation was different for 2-aminooxyacetic acid and 2-amino-4-methoxy-3-butenoic acid.

References

Gatehouse P, Hopper S, Schatz L, SEGAL H . Further characterization of alanine aminotransferase of rat liver. J Biol Chem. 1967; 242(10):2319-24. View

Gutierrez M, Gracen V, Edwards G . Biochemical and cytological relationships in C4 plants. Planta. 2014; 119(4):279-300. DOI: 10.1007/BF00388331. View

Davis B . DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964; 121:404-27. DOI: 10.1111/j.1749-6632.1964.tb14213.x. View

Hatch M . Separation and properties of leaf aspartate aminotransferase and alanine aminotransferase isoenzymes operative in the C4 pathway of photosynthesis. Arch Biochem Biophys. 1973; 156(1):207-14. DOI: 10.1016/0003-9861(73)90358-5. View

CRUICKSHANK D, ISHERWOOD F . Glutamic-alanine and glutamic-aspartic transaminases of wheat germ. Biochem J. 1958; 69(2):189-95. PMC: 1196537. DOI: 10.1042/bj0690189. View

Cornell N, Crow K, Whitefoot R . Re-activation by glutamate or aspartate of amino-oxyacetate-inhibited aspartate aminotransferase in vitro and in isolated hepatocytes. Biochem J. 1981; 198(1):219-23. PMC: 1163230. DOI: 10.1042/bj1980219. View

Hopper S, SEGAL H . Kinetic studies of rat liver glutamicalanine transaminase. J Biol Chem. 1962; 237:3189-95. View

Smith S, Freedland R . Functional inhibition of cytosolic and mitochondrial aspartate aminotransferase by L-2-amino-4-methoxy-trans-3-butenoic acid in isolated rat hepatocytes and mitochondria. Arch Biochem Biophys. 1981; 209(2):335-41. DOI: 10.1016/0003-9861(81)90289-7. View

Hatch M, Mau S . Activity, location, and role of asparate aminotransferase and alanine aminotransferase isoenzymes in leaves with C4 pathway photosynthesis. Arch Biochem Biophys. 1973; 156(1):195-206. DOI: 10.1016/0003-9861(73)90357-3. View

10.

Soper T, Manning J, Marcotte P, WALSH C . Inactivation of bacterial D-amino acid transaminases by the olefinic amino acid D-vinylglycine. J Biol Chem. 1977; 252(5):1571-5. View

11.

Arnon D . COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS. Plant Physiol. 1949; 24(1):1-15. PMC: 437905. DOI: 10.1104/pp.24.1.1. View

12.

Ovchinnikov Y, Egorov C, Aldanova N, Feigina M, Lipkin V, Abdulaev N . The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heart. FEBS Lett. 1973; 29(1):31-34. DOI: 10.1016/0014-5793(73)80008-0. View

13.

Ford G, Eichele G, Jansonius J . Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase. Proc Natl Acad Sci U S A. 1980; 77(5):2559-63. PMC: 349441. DOI: 10.1073/pnas.77.5.2559. View

14.

Rando R . Irreversible inhibition of aspartate aminotransferase by 2-amino-3-butenoic acid. Biochemistry. 1974; 13(19):3859-63. DOI: 10.1021/bi00716a006. View

15.

Rando R, Relyea N, Cheng L . Mechanism of the irreversible inhibition of aspartate aminotransferase by the bacterial toxin L-2-amino-4-methoxy-trans-3-butenoic acid. J Biol Chem. 1976; 251(11):3306-12. View

16.

Bradford M . A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248-54. DOI: 10.1016/0003-2697(76)90527-3. View

17.

Doonan S, Doonan H, Hanford R, Vernon C, Walker J, da Airold L . The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues. Biochem J. 1975; 149(3):497-506. PMC: 1165654. DOI: 10.1042/bj1490497d. View

18.

Gehring H, Rando R, Christen P . Active-site labeling of aspartate aminotransferases by the beta,gamma-unsaturated amino acid vinylglycine. Biochemistry. 1977; 16(22):4832-6. DOI: 10.1021/bi00641a012. View

19.

KAGAMIYAMA H, Teranishi K, Tanase S, Morino Y, Sakakibara R, Wada H . Complete amino acid sequence of mitochondrial aspartate aminotransferase from pig heart muscle. Tryptic peptides. J Biol Chem. 1980; 255(13):6138-43. View