Khristoforov R R, Sukhareva B S, Dixon H B, Sparkes M J, Krasnov V P, Bukrina I M
Engelhardt Institute of Molecular Biology, RAN, Moscow, Russia.
Biochem Mol Biol Int. 1995 May;36(1):77-85.
The interaction of glutamate decarboxylase with the aspartate analogues 3-arsonoalanine and 3-phosphonoalanine, with the glutamate analogues 2-amino-4-arsonobutyric acid and 2-amino-4-phosphonobutyric acid, and with 4-(methylthio)-L-glutamic acid, both as a mixture of diastereoisomers and as the (2S,4R)-form, was studied. All these analogues were poor substrates for the enzyme and only weak inhibitors. Their decarboxylation was accompanied by transamination of the enzyme-bound pyridoxal phosphate (PLP) to pyridoxamine phosphate (PMP), thus inactivating the decarboxylase. With arsonoalanine only part of the PLP was converted into PMP.
研究了谷氨酸脱羧酶与天冬氨酸类似物3-胂基丙氨酸和3-膦酰基丙氨酸、谷氨酸类似物2-氨基-4-胂基丁酸和2-氨基-4-膦酰基丁酸以及4-(甲硫基)-L-谷氨酸（以非对映异构体混合物形式以及(2S,4R)-形式）的相互作用。所有这些类似物都是该酶的不良底物且只是弱抑制剂。它们的脱羧伴随着酶结合的磷酸吡哆醛（PLP）转氨生成磷酸吡哆胺（PMP），从而使脱羧酶失活。对于胂基丙氨酸，只有部分PLP转化为PMP。
Zotero 插件