Biochemical and Genetic Characterization of an FK506-Sensitive Peptidyl Prolyl cis-trans Isomerase from a Thermophilic Archaeon, Methanococcus thermolithotrophicus

A peptidyl prolyl cis-trans isomerase (PPIase) was purified from a thermophilic methanogen, Methanococcus thermolithotrophicus. The PPIase activity was inhibited by FK506 but not by cyclosporine. The molecular mass of the purified enzyme was estimated to be 16 kDa by sodium dodecyl sulfate-polyacryl...

Täydet tiedot

Bibliografiset tiedot

Julkaisussa:	J Bacteriol
Päätekijät:	Furutani, Masahiro, Iida, Toshii, Yamano, Shigeyuki, Kamino, Kei, Maruyama, Tadashi
Aineistotyyppi:	Artigo
Kieli:	Inglês
Julkaistu:	American Society for Microbiology (ASM) 1998
Aiheet:	Enzymes and Proteins
Linkit:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC106894/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9440528/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.180.2.388-394.1998
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