Purification and Characterization of a 4-Hydroxybenzoate Decarboxylase fromChlamydophila pneumoniaeAR39
β Scribed by J. Liu; X. Zhang; S. Zhou; P. Tao; J. Liu
- Publisher
- Springer
- Year
- 2007
- Tongue
- English
- Weight
- 178 KB
- Volume
- 54
- Category
- Article
- ISSN
- 0343-8651
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Two 4-hydroxybenzoate decarboxylase activities and a phenol carboxylase activity were found in cell-free extracts of a defined, 4-hydroxybenzoate-or phenol-grown consortium. Both decarboxylase activities were loosely membrane-associated and required K Γ· but a different pH and ion strength. Loss of a
The ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases) are a family of enzymes that control the levels of extracellular nucleotides, thereby modulating purinergically controlled physiological processes. Six of the eight known NTPDases are membrane-bound enzymes; only NTPDase 5 and 6 can be