Potential turnover rate of traffic ATPases
| Range | 1 to 10 1/sec |
|---|---|
| Organism | prokaryote |
| 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 right column top paragraphPubMed ID9346917 |
| Comments | "The evidence obtained from several prokaryotic systems suggests several general properties of traffic ATPases: association between the two nucleotide-binding domains leading to cooperativity, regulation of ATPase activity by the hydrophobic components and phospholipids, affinity for ATP in the range of 100–200 µM, and potential turnover rate of 1–10 s^-1." |
| Entered by | Uri M |
| ID | 109035 |