Structures of Pyruvoyl-Dependent Histidine Decarboxylase and Mutant-3 Prohistidine Decarboxylase from Lactobacillus 30A
In man, the decarboxylatlon of histidine to form histamine is most often associated with the clinical treatment of colds, allergies, and ulcers. However, mammalian histidine decarboxylase activity is low, and attempts to isolate and characterize it have been frustrated by instability (Boeker and Snell, 1972; Snell, 1977; Tran and Snyder, 1981) . On the other hand, much histidine decarboxylase activity is found in mammalian intestines due to the presence of lactic acid bacteria similar to Lactobacillus 30a. This organism produces large amounts of histidine decarboxylase, which has been studied extensively. Although the biological function of the histamine produced is not yet understood, histamine is known to be a powerful regulator of the vascular and digestive systems. Histamine of bacterial origin may cause a selective advantage to the microorganisms by altering the physiology of the host (Recsei and Snell, 1984).
KeywordsPyridoxal Phosphate Histidine Decarboxylase Mammalian Intestine Histidine Decarboxylase Activity Chemical Molecular Weight
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