|
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 |
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