| Value |
1
1/sec
|
| Organism |
Bacteria Escherichia coli |
| 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 3rd paragraphPubMed ID9346917
|
| Primary Source |
Koronakis V, Hughes C, Koronakis E. ATPase activity and ATP/ADP-induced conformational change in the soluble domain of the bacterial protein translocator HlyB. Mol Microbiol. 1993 Jun8(6):1163-75.PubMed ID8361361
|
| Comments |
"The nucleotide-binding domain of the E. coli hemolysin
exporter, HlyB, purified as a soluble fusion protein containing
glutathione S-transferase at its amino terminus (GST-Bctp)
(primary source), has a Km value for ATP of 200µM and a turnover number
of 1s^-1." |
| Entered by |
Uri M |
| ID |
109034 |