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  • Title: [Effects of pyridoxal-phosphate and its 4'- and 5'-substituted analogs on macromolecular structure of Escherichia coli glutamate decarboxylase].
    Author: Kulikova AI, Sukhareva BS, L'vova SD, Stepanova SV, Gunar VI.
    Journal: Mol Biol (Mosk); 1982; 16(3):585-92. PubMed ID: 7048067.
    Abstract:
    Interactions of pyridoxal phosphate and its analogs (at pH 6.0) with dimeric glutamate apodecarboxylase (E. coli) were examined by spectrophotometric and CD-titration and by gel electrophoresis. It was shown that 5 equivalents of pyridoxal-phosphate fully restore the catalytic activity and optical properties of the enzyme, whereas 3 equivalents of the coenzyme suffice for reconstitution of the hexameric structure. Similar amounts of the 2 nor PLP adn 5'-methtyl PLP restore the hexameric macromolecule. 15 equivalents of pyridoxine phosphate or 54 -- of pyridoxamine phosphate are required for complete saturation of the apoenzymes binding sites and concomitant reconstitution of the hexameric structure. 5'-deoxy-5'-carboxymethyl pyridoxal, 5'-deoxy-5'-phosphonomethyl pyridoxal and cis-5'-deoxy-5'-phosphonomethylen pyridoxal were merely bound to the dimeric apoenzyme, but failed to restore the enzyme's quaternary structure. Pyridoxal, trans-5'-deoxy-5'-posphonomethylen pyridoxal and pyridoxine analogs substituted in position 5' with carboxyl or phosphonyl group did not interact with the apodecarboxylase.
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