Purification and properties of an acylamide amidohydrolase (E. C. 3.5.1.4) with a wide activity spectrum from Brevibacterium sp. R 312
✍ Scribed by A. Thiery; M. Maestracci; Dr. A. Arnaud; P. Galzy; M. Nicolas
- Publisher
- John Wiley and Sons
- Year
- 1986
- Tongue
- English
- Weight
- 781 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0233-111X
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✦ Synopsis
An amidase with a wide activity spectrum was purified from the Brevibacterium sp. R 312 and studied. The purification was performed by precipitating the proteins of the supernatant fraction obtained after centrifugation of sonicated cells. The resulting proteins were submitted to a gel filtration step followed by DEAE-Sephadex ion exchange chromatography and then by another gel filtration process. The purified amidase had a molecular weight of 180,000 and was composed of four subunits of the same molecular weight (43,000 2,000). Its isoelectric point was 3.5. This enzyme was able to hydrolyze a large number of amides into their corresponding organic acids and it also possessed an acyl transferase activity.
Amidases, and especially microbial amidases, have been extensively studied (CLARKE 1970). These enzymes seem t o be very wide spread among protists: bacteria (CLARKB