Purification and properties of histidine decarboxylase from Lactobacillus 30a.
- 1 July 1965
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 54 (1), 152-158
- https://doi.org/10.1073/pnas.54.1.152
Abstract
The histidine decarboxylase from Lactobacillus 30a was obtained in crystalline and apparently homogeneous form. Only L-histidine serves as substrate; several imidazole compounds are effective competitive inhibitors. Cyanide inhibits noncompetitively. The spectrum of the pure enzyme is that of a simple protein; the enzyme is not dependent upon pyridoxal phosphate as a cofactor unlike other amino-acid decarboxylases.Keywords
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