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...

The lysA gene encodes meso-diaminopimelate (DAP) decarboxylase (E.C.4.1.1.20), the last enzyme of the lysine biosynthetic pathway in bacteria. We have determined the nucleotide sequence of the lysA gene from Pseudomonas aeruginosa. Comparison of the deduced amino acid sequence of the lysA gene product revealed extensive similarity with the sequences of the functionally equivalent enzymes from E...

Mammalian histidine decarboxylases have not been characterized well owing to their low amounts in tissues and instability. We describe here the first spectroscopic characterization of a mammalian histidine decarboxylase, i.e. a recombinant version of the rat enzyme purified from transformed Escherichia coli cultures, with similar kinetic constants to those reported for mammalian histidine decar...

Mammalian organs are known to decarboxylate a number of n-amino acids. Of the mammalian decarboxylases, 3,4-dihydroxyphenylalanine decarboxylase is probably the most studied. Blaschko (1) reported values for DOPAl decarboxylase in .liver and kidney of several animal species. The enzyme was shown to be deactivated by dialysis and its activity restored by the addition of pyridoxal phosphate (2, 3...

During the course of infection, Salmonella enterica serovar Typhimurium must successively survive the harsh acid stress of the stomach and multiply into a mild acidic compartment within macrophages. Inducible amino acid decarboxylases are known to promote adaptation to acidic environments. Three low pH inducible amino acid decarboxylases were annotated in the genome of S. Typhimurium, AdiA, Cad...

Mammalian organs are known to decarboxylate a number of n-amino acids. Of the mammalian decarboxylases, 3,4-dihydroxyphenylalanine decarboxylase is probably the most studied. Blaschko (1) reported values for DOPAl decarboxylase in .liver and kidney of several animal species. The enzyme was shown to be deactivated by dialysis and its activity restored by the addition of pyridoxal phosphate (2, 3...

Histamine poisoning is caused by the ingestion of food containing high levels of histamine, a biogenic amine. Histamine could be expected in virtually all foods that contain proteins or free histidine and that are subject to conditions enabling microbial activity. In most histamine-containing foods the majority of the histamine is generated by decarboxylation of the histidine through histidine ...