Inactivation of pyridoxal phosphate enzymes by gabaculine. Correlation with enzymic exchange of beta-protons.
作者： T S Soper , J M Manning
DOI: 10.1016/S0021-9258(19)45322-2
关键词: D-Alanine Transaminase 、 Stereochemistry 、 Tryptophanase 、 Gabaculine 、 Enzyme 、 Transaminase 、 Active site 、 Pyridoxal phosphate 、 Chemistry 、 Alanine racemase 、 Biochemistry 、 Cell biology 、 Molecular biology
摘要: Gabaculine, 5-amino-1,3-cyclohexadienylcarboxylate, is a very efficient enzyme-activated inhibitor of gamma-aminobutyrate transaminase (Rando, R. (1977) Biochemistry 16, 4604-4610). However, enzymes for which not substrate are also inactivated by gabaculine. Thus, purified D-amino acid transaminase, L-alanine and L-aspartate (Ki values 0.1 mM, 1 55 respectively). The effects this on such diverse group appear to be related the enzymic exchange beta-protons their normal substrates. L-Alanine known catalyze an (Walter, U., Luthe, H., Gerhart, F., Soling, H.-D. (1975) Eur. J. Biochem. 59, 395-403). D-Amino gabaculine, Alanine racemase tryptophanase, analogous exchange, were found insensitive We postulate that aromatization in beta-proton removed, enzyme-catalyzed event those pyridoxal phosphate have nucleophilic at active site process.
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sci-hub.st 参考文章(53)
L.L. Henderson, R.B. Johnston, Inhibition studies of the enantiomers of β chloroalanine on purified Alanine Racemase from B.subtilis Biochemical and Biophysical Research Communications. ,vol. 68, pp. 793- 798 ,(1976) , 10.1016/0006-291X(76)91215-8
Robert R. Rando, F.W. Bangerter, The in vivo inhibition of gaba-transaminase by gabaculine Biochemical and Biophysical Research Communications. ,vol. 76, pp. 1276- 1281 ,(1977) , 10.1016/0006-291X(77)90993-7
Communicative Disorders, Thomas Newell Chase, Donald Bayley Tower, Eugene Roberts, GABA in nervous system function Raven Press. ,(1976)
Yoshimasa Morino, Abdalla Mohamed Osman, Mitsuhiro Okamoto, Formate-induced Labeling of the Active Site of Aspartate Aminotransferase by β-Chloro-l-alanine Journal of Biological Chemistry. ,vol. 249, pp. 6684- 6692 ,(1974) , 10.1016/S0021-9258(19)42208-4
A J Cooper, Proton magnetic resonance studies of glutamate-alanine transaminase-catalyzed deuterium exchange. Evidence for proton conservation during prototropic transfer from the alpha carbon of L-alanine to the C4-position of pyridoxal 5'-phosphate. Journal of Biological Chemistry. ,vol. 251, pp. 1088- 1096 ,(1976) , 10.1016/S0021-9258(17)33805-X
N Seiler, M J Jung, Enzyme-activated irreversible inhibitors of L-ornithine:2-oxoacid aminotransferase. Demonstration of mechanistic features of the inhibition of ornithine aminotransferase by 4-aminohex-5-ynoic acid and gabaculine and correlation with in vivo activity. Journal of Biological Chemistry. ,vol. 253, pp. 7431- 7439 ,(1978) , 10.1016/S0021-9258(17)34520-9
Milton H. Saier, W. Terry Jenkins, Alanine Aminotransferase: I. PURIFICATION AND PROPERTIES Journal of Biological Chemistry. ,vol. 242, pp. 91- 100 ,(1967) , 10.1016/S0021-9258(18)96322-2
Y. Morino, H. Kojima, S. Tanase, Affinity labeling of alanine aminotransferase by 3-chloro-L-alanine. Journal of Biological Chemistry. ,vol. 254, pp. 279- 285 ,(1979) , 10.1016/S0021-9258(17)37915-2
G. Burnett, K. Yonaha, S. Toyama, K. Soda, C. Walsh, Studies on the kinetics and stoichiometry of inactivation of Pseudomonas omega-amino acid:pyruvate transaminase by gabaculine. Journal of Biological Chemistry. ,vol. 255, pp. 428- 432 ,(1980) , 10.1016/S0021-9258(19)86191-4
J.E. Churchich, U. Moses, 4-Aminobutyrate aminotransferase. The presence of nonequivalent binding sites. Journal of Biological Chemistry. ,vol. 256, pp. 1101- 1104 ,(1981) , 10.1016/S0021-9258(19)69931-X