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...

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Hlavní autoři: Story, Sherry V., Grunden, Amy M., Adams, Michael W. W.
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Microbiology 2001
Témata:
Enzymes and Proteins
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC95316/
https://ncbi.nlm.nih.gov/pubmed/11418567
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JB.183.14.4259-4268.2001
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