Turnover rate of MalK, the nucleotide-binding component of maltose permease
| Value | 0.9 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 3rd paragraphPubMed ID9346917 |
| Comments | "MalK, the nucleotide-binding component of the maltose permease, has been purified via a denaturation-renaturation of inclusion bodies (22) it has a turnover rate of 0.9s^-1 (calculated from Ref. 33 [PMID 8360157], assuming that it functions as a monomer) and an affinity for ATP of 70 µM, both of which are comparable to those of HisP(his6)." |
| Entered by | Uri M |
| ID | 109033 |