Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases
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چکیده
منابع مشابه
Purification and properties of pyridoxal-5'-phosphate-dependent histidine decarboxylases from Klebsiella planticola and Enterobacter aerogenes.
Histidine decarboxylases from Klebsiella planticola and Enterobacter aerogenes were purified to homogeneity and compared with the histidine decarboxylase from Morganella morganii. All three enzymes required pyridoxal 5'-phosphate as a coenzyme, showed optimal activity at pH 6.5, decarboxylated only histidine among the amino acids derived from protein, and were tetramers or dimers of identical s...
متن کاملA novel pyridoxal 5'-phosphate-dependent amino acid racemase in the Aplysia californica central nervous system.
D-aspartate (D-Asp) is found in specific neurons, transported to neuronal terminals and released in a stimulation-dependent manner. Because D-Asp formation is not well understood, determining its function has proved challenging. Significant levels of D-Asp are present in the cerebral ganglion of the F- and C-clusters of the invertebrate Aplysia californica, and D-Asp appears to be involved in c...
متن کاملPyridoxal 5”Phosphate-dependent Histidine Decarboxylase
Pyridoxal phosphate-dependent histidine decarboxylase from Morganella morganii AM-15 was inactivated by (a-a-fluoromethylhistidine by a pseudo firstorder reaction, with KI and kinact values of 0 . 1 mM and 32.2 min-l, respectively, and was most efficient at pH 6.5-7.0. Both L-histidine and the competitive inhibitor, L-histidine methyl ester, protected against inactivation. The apoenzyme was not...
متن کاملThe reaction of amino-oxyacetate with pyridoxal phosphate-dependent enzymes.
The carbonyl reagent amino-oxyacetate is frequently used in metabolic studies to inhibit individual pyridoxal phosphate enzymes. The reaction of this compound with three such enzymes, aspartate transaminase, 4-aminobutyrate transaminase and dopa (3,4-dihydroxyphenylalanine) decarboxylase, was studied to determine the extent to which the inhibition is reversible and the rates at which it takes p...
متن کاملIdentification of amino acid residues modified by pyridoxal 5'-phosphate in Escherichia coli glutamine synthetase.
Chemical modification studies with pyridoxal 5'-phosphate have indicated that lysine(s) appear to be at or near the active site of Escherichia coli glutamine synthetase (Colanduoni, J., and Villafranca, J. J. (1985) J. Biol. Chem. 260, 15042-15050; Whitley, E. J., Jr., and Ginsburg, A. (1978) J. Biol. Chem. 253, 7017-7025). Enzyme samples were prepared that contained approximately 1, approximat...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1994
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1994.tb18816.x