Studies on bacterial amino-acid decarboxylases

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Abstract
The extrac-tion, purification, and properties of 1 ( [long dash])-histidine decar-boxylase from a strain of Clostridium welchii Type A are descr. Acetone powders and enzyme prepns. specifically attack 1( [long dash]) -histidine, which is decarboxylated quantitatively to histamine. The activity is the same in acetate or phthalate buffer systems, the opt. being at pH 4.5. Rate of the reaction bears a linear relation to the amount of enzyme prepn. used. M/100 sulfanilamide specifically caused 51% inhibition which is not reversed by addition to the enzyme prepn. of [rho]-aminobenzoic acid or of a boiled aqueous suspension of Cl. welchii. The enzyme appears to be devoid of codecarboxylase.

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