Purification and properties of serine hydroxymethyltransferase from Sulfolobus solfataricus.

Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to glycine with the transfer of the one-carbon group to tetrahydrofolate to form 5,10-methylenetetrahydrofolate. No SHMT has been purified from a nonmethanogenic Archaea strain, in part because this group of organisms...

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Библиографические подробности

Опубликовано в::	J Bacteriol
Главные авторы:	Delle Fratte, S, White, R H, Maras, B, Bossa, F, Schirch, V
Формат:	Artigo
Язык:	Inglês
Опубликовано:	American Society for Microbiology (ASM) 1997
Предметы:	Research Article
Online-ссылка:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC179697/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9393711/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.179.23.7456-7461.1997
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