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• W1899401069 abstract "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 subunits. Amino-terminal sequences of the three enzymes showed up to 81% homology through residue 33, but the enzymes differed sufficiently in amino acid composition and sequence so that no cross-reaction occurred between the K. planticola or E. aerogenes enzymes and antibodies to the decarboxylase from M. morganii. All three enzymes were inhibited by carbonyl reagents; by amino-, carboxyl-, and some methyl-substituted histidines; and by alpha-fluoromethylhistidine. These decarboxylases, all from gram-negative organisms, differed greatly in subunit structure, biogenesis, and other properties from the pyruvoyl-dependent histidine decarboxylases from gram-positive organisms described previously." @default.
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• W1899401069 date "1987-09-01" @default.
• W1899401069 modified "2023-09-23" @default.
• W1899401069 title "Purification and properties of pyridoxal-5'-phosphate-dependent histidine decarboxylases from Klebsiella planticola and Enterobacter aerogenes" @default.
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• W1899401069 doi "https://doi.org/10.1128/jb.169.9.3963-3968.1987" @default.
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