Characterization of an Aminoacylase from the Hyperthermophilic Archaeon Pyrococcus furiosus
Aminoacylase was identified in cell extracts of the hyperthermophilic archaeon Pyrococcus furiosus by its ability to hydrolyze N-acetyl-l-methionine and was purified by multistep chromatography. The enzyme is a homotetramer (42.06 kDa per subunit) and, as purified, contains 1.0 ± 0.48 g-atoms of zin...
محفوظ في:
| الحاوية / القاعدة: | J Bacteriol |
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| المؤلفون الرئيسيون: | , , |
| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
American Society for Microbiology (ASM)
2001
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| الموضوعات: | |
| الوصول للمادة أونلاين: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC95316/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11418567/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/JB.183.14.4259-4268.2001 |
| الوسوم: |
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