Reverse Gyrase from the Hyperthermophilic Bacterium Thermotoga maritima: Properties and Gene Structure

The hyperthermophilic bacterium Thermotoga maritima MSB8 possesses a reverse gyrase whose enzymatic properties are very similar to those of archaeal reverse gyrases. It catalyzes the positive supercoiling of the DNA in an Mg(2+)- and ATP-dependent process. Its optimal temperature of activity is arou...

Celý popis

Podrobná bibliografie

Vydáno v:	J Bacteriol
Hlavní autoři:	de la Tour, Claire Bouthier, Portemer, Christiane, Kaltoum, Habib, Duguet, Michel
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1998
Témata:	Enzymes and Proteins
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC106882/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9440516/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.180.2.274-281.1998
Tagy:	Přidat tag Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!