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Labilization of the phospho ester bond in enzyme inhibitor complexes of aspartate glutamate trans aminase



Labilization of the phospho ester bond in enzyme inhibitor complexes of aspartate glutamate trans aminase



Molekulyarnaya Biologiya (Moscow) 10(4): 897-906



Individual enzyme-inhibitor complexes having characteristic absorption spectra were obtained after interaction between the apoenzyme of aspartate aminotransferase [pig heart] and N.alpha.-(5'-Phosphopyridoxyl)-L-glutamic acid, N.alpha.-(5'-Phosphopyridoxyl)-D-glutamic acid, and N.alpha.-5'-Phosphopyridoxyl)-2-oxopyrrolidine-5-carboxylic acid. Stability of enzyme-inhibitor complexes was studied under various conditions: reactivation by the coenzyme, denaturation by urea and pH variation. The complexes formed by the 2 latter inhibitors are reactivated by pyridoxal-5'-phosphate. The inhibitor may be released under mild conditions. The enzyme-inhibitor complex formed by N.alpha.-(5'-Phosphopyridoxyl)-L-glutamic acid, was not reactivated by the coenzyme. Pyridoxylglutamic acid was isolated during the attempt to release the inhibitor. The process of dephosphorylation of the inhibitor was connected with enzyme-involved hydrolysis of phosphate bond as well as with phosphorylation of aspartate-aminotransferase. A 32P-peptide, containing 13 amino acids was isolated after tryptic digestion of enzyme-inhibitor complex formed with 32P-inhibitor. A conclusion was drawn about the active role of phosphate group of the coenzyme in the reaction enzymatic transamination. This conclusion was confirmed by the study of properties of enzyme-inhibitor complex formed between 32P-aspartate aminotransferase and threocycloglutamic acid and by investigating borohydride reducing reaction of 32P-aspartate aminotransferase.

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