Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri.

The 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri was purified 313-fold to a specific activity of 470 mumol min-1 mg-1 at 37 degrees C and pH 7.8. At this stage, the enzyme was pure as judged from polyacrylamide gel electrophoresis. The monofunctional enzyme was oxy...

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Vydáno v:	J Bacteriol
Hlavní autoři:	te Brömmelstroet, B W, Hensgens, C M, Geerts, W J, Keltjens, J T, van der Drift, C, Vogels, G D
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1990
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC208478/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2298699/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.172.2.564-571.1990
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