| Range |
~0.008 1/sec
|
| Organism |
Eukaryotes |
| 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 4th paragraphPubMed ID9346917
|
| Primary Source |
Ko YH, Pedersen PL The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase. J Biol Chem. 1995 Sep 22 270(38):22093-6.PubMed ID7545672
|
| Comments |
"Among eukaryotic traffic ATPases, a comparison can be
made with one of the nucleotide-binding domains of CFTR (the
amino-terminal one) which has been characterized in vitro as a
soluble protein fused to the maltose-binding protein (primary source). Its
affinity for ATP is 110µM and comparable to that of the
prokaryotic systems its activity, 0.008 s^-1, is much lower
than that of the prokaryotic subunits, possibly due to the fact
that since the membrane-spanning and nucleotide-binding domains
of CFTR normally form a single protein, their ability to
impart positive regulatory stimuli may have been eliminated in
the chimeric product." CFTR=cystic fibrosis transmembrane conductance regulator |
| Entered by |
Uri M |
| ID |
109036 |