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Purification and Properties of a Fructose-1,6-Diphosphate-Activated Lactate Dehydrogenase from Streptococcus faecalis

An l-(+)-lactate dehydrogenase was purified approximately 35-fold from crude extracts of Streptococcus faecalis. The purified enzyme had an absolute and specific requirement for fructose-1,6-diphosphate (FDP) for catalytic activity. The concentration of FDP required for 50% maximal activity was abou...

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Vydáno v:J Bacteriol
Hlavní autoři: Wittenberger, Charles L., Angelo, Noreen
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Microbiology (ASM) 1970
Témata:
On-line přístup:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC250383/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/4314543/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.101.3.717-724.1970
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