[A model of enzymatic decarboxylation of glutamic acid].
Interaction of glutamate decarboxylase with its adequate substrate and some quasi-substrates was studied by spectrokinetic, quantum-chemical and some other approaches. It was shown that in the course of decarboxylation an abortive transamination of pyridoxal-5'-phosphate leading to the enzyme inactivation does occur. Identification of intermediate coenzyme-substrate complexes allowed to formulate a model of enzymatic decarboxylation taking into account both the main and abortive reactions. The analysis of electronic structure of the intermediates revealed some of the factors determining the functional specificity of the reaction under study.
Almazov
V P
VP
Morozov
Iu V
IuV
Savin
F A
FA
Sukhareva
B S
BS
D002942:Circular Dichroism; D003653:Decarboxylation; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D005968:Glutamate Decarboxylase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D005971:Glutamates / Q000378:metabolism*; D018698:Glutamic Acid; D007700:Kinetics; D008956:Models, Chemical; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000378:metabolism; D013379:Substrate Specificity
D005971:Glutamates; D018698:Glutamic Acid; D011732:Pyridoxal Phosphate; D005968:Glutamate Decarboxylase
Model' fermentativnogo dekarboksilirovaniia glutaminovoĭ kisloty.