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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Bibliografske podrobnosti

izdano v:	J Bacteriol
Principais autores:	Story, Sherry V., Grunden, Amy M., Adams, Michael W. W.
Format:	Artigo
Jezik:	Inglês
Izdano:	American Society for Microbiology (ASM) 2001
Teme:	Enzymes and Proteins
Online dostop:	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
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