Вид документа : Статья из журнала Шифр издания : 54/D 29 Автор(ы) : Khristoforov R. R., Suchareva B. S., Dixon H. B. F., Sparkers M. J., Krasnov V. P., Bukrina I. M., Grishakov A. N. Заглавие : Decarboxylation and side transamination when glutamate decarboxylase from Escherichia coli acts on substrate analogues modified at C-3 and C-4 Место публикации : Biochemistry. - 1996. - Vol. 61, N 3. - С. 343-348 ББК : 54 Предметные 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. Доп.точки доступа: Khristoforov, R. R.; Suchareva, B. S.; Dixon, H. B. F.; Sparkers, M. J.; Krasnov, V. P.; Bukrina, I. M.; Grishakov, A. N.