D 29 Decarboxylation and side transamination when glutamate decarboxylase from Escherichia coli acts on substrate analogues modified at C-3 and C-4 [Text] / R. R. Khristoforov, B. S. Suchareva, H. B. F. Dixon, M. J. Sparkers, V. P. Krasnov, I. M. Bukrina, A. N. Grishakov // Biochemistry. - 1996. - Vol. 61, N 3. - P343-348 Рубрики: ХИМИЧЕСКИЕ НАУКИ Аннотация: The interaction of glutamate decarboxylase with aspartate and glutamate analogues modified at C-3 and C-4 was studied. 3-Arsonoalanine, 3-phosphonoalanine, 2-amino-4-arsonobutyric acid, 2-amino-4-phospho-nobutyric acid, a mixture of diastereoisomers of 4-(methylthio)glutamic acid, and erythro-4-(methylthio)glutamic acid were shown to be poor substrates for the enzyme. |