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Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantioselectively hydrolyzes 2-arylpropionamides.
An enantioselective amidase from Rhodococcus erythropolis MP50 was purified to homogeneity. The enzyme has a molecular weight of about 480,000 and is composed of identical subunits with molecular weights of about 61,000. The NH2-terminal amino acid sequence was significantly different from previousl...
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| Main Authors: | , , |
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| 格式: | Artigo |
| 語言: | Inglês |
| 出版: |
1996
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| 主題: | |
| 在線閱讀: | https://ncbi.nlm.nih.gov/pmc/articles/PMC178119/ https://ncbi.nlm.nih.gov/pubmed/8655547 |
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