type	Journal Article
authors	Rosenfeld, H. J.; Roberts, J.
title	Arginine decarboxylase from a Pseudomonas species
journal	J Bacteriol
Activity	4.1.1.19
ui	76094943
year	(1976)
volume	125
number	2
pages	601-7.
keywords	Aminooxyacetic Acid/pharmacology
abstract	An arginine decarboxylase has been isolated from a Pseudomonas species. The enzyme is constitutive and did not appear to be repressed by a variety of carbon sources. After an approximately 40-fold purification, the enzyme appeared more similar in its properties to the Escherichia coli biosynthetic arginine decarboxylase than to the E. coli inducible (biodegradative) enzyme. The Pseudomonas arginine decarboxylase exhibited a pH optimum of 8.1 and an absolute requirement of Mg2+ and pyridoxal phosphate, and was inhibited significantly at lower Mg2+ concentrations by the polyamines putrescine, spermidine, and cadaverine. The Km for L-arginine was about 0.25 mM at pH 8.1 AND 7.2. The enzyme was completely inhibited by p-chloromercuribenzoate. The inhibition was prevented by dithiothreitol, a feature that suggests the involvement of an -SH group. Of a variety of labeled amino acids tested, only L-arginine, but not D-arginine was decarboxylated. D- Arginine was a potent inhibitor of arginine decarboxylase with a Ki of 3.2 muM.
last changed	2002/11/12 16:17