| Range |
~0.3 1/sec
|
| Organism |
Bacteria Salmonella typhimurium |
| Reference |
Nikaido K, Liu PQ, Ames GF. Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activity. J Biol Chem. 1997 Oct 31 272(44):27745-52. p.27752 left column 2nd paragraphPubMed ID9346917
|
| Primary Source |
Liu CE, Liu PQ, Ames GF. Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter). J Biol Chem. 1997 Aug 29 272(35):21883-91.PubMed ID9268321
|
| Comments |
"...This value [2sec^-1] is higher
than that observed for the intrinsic activity of the complex
(about 0.3 s^-1 (primary source)), which is consistent with the notion that in
the absence of HisQ and HisM the activity of HisP is relieved." Please note-value wasn't located in primary source |
| Entered by |
Uri M |
| ID |
109031 |