Besides its nitrile hydratase and wide spectrum amidase activities, the Brevibacterium sp. R312 strain also possesses a constitutive beta-glucosidase. Its optimum pH is 6. The enzyme was purified by fractionation precipitation with ammonium sulfate followed by chromatographic elutions on Q-Sepharose
The N-terminal amino acid sequences of Brevibacterium sp. R312 nitrile hydratase
β Scribed by R. Duran; C. K. N. Chan Kwo Chion; F. Bigey; Prof. A. Arnaud; P. Galzy
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- English
- Weight
- 608 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0233-111X
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β¦ Synopsis
Abstract
Nitrile hydratase from Brevibacterium sp. R312 was purified to homogeneity. The isoelectric point was 5.75. The two kinds of subunits were separated by reverse phase HPLC and their Nβterminal amino acid sequences were found to be identical to those of Rhodococcus sp. Nβ774 nitrile hydratase.
π SIMILAR VOLUMES
3-Amino-2-hydroxydecanoic acid (AHDA) is a novel amino acid which has been suggested as the Nterminal component of the recently isolated angiotensin-converting "enzyme inhibitor microginin. The naturally occurring amino acid was found to possess syn relative stereochemistry and (2S,3R) absolute ster