Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.4.2.1 extracted from

  • Liu, P.Q.; Liu, C.E.; Ferro-Luzzi Ames, G.
    Modulation of ATPase activity by physical disengagement of the ATP-binding domains of an ABC transporter, the histidine permease (1999), J. Biol. Chem., 274, 18310-18318.
    View publication on PubMed
Search for more literature for 7.4.2.1

Protein Variants

Protein Variants Comment Organism
D61N mutation in the ATP-binding subunit HisP*, defective in ATP hydrolysis Salmonella enterica subsp. enterica serovar Typhimurium
E191K mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme. Increased intrinsic ATPase activity without HisJ Salmonella enterica subsp. enterica serovar Typhimurium
E202K mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme. Increased intrinsic ATPase activity without HisJ Salmonella enterica subsp. enterica serovar Typhimurium
H211R mutation in the ATP-binding subunit HisP*, defective in ATP hydrolysis Salmonella enterica subsp. enterica serovar Typhimurium
K45P mutation in the ATP-binding subunit HisP*, defective in ATP hydrolysis Salmonella enterica subsp. enterica serovar Typhimurium
additional information mutations in the ATP-binding subunit that allow ligand translocation and ATP hydrolysis in the absence of the binding protein Salmonella enterica subsp. enterica serovar Typhimurium
P172T mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme Salmonella enterica subsp. enterica serovar Typhimurium
P172T increased intrinsic ATPase activity without HisJ Salmonella enterica subsp. enterica serovar Typhimurium
T205A mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme Salmonella enterica subsp. enterica serovar Typhimurium
T205M mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme Salmonella enterica subsp. enterica serovar Typhimurium
T205M increased intrinsic ATPase activity without HisJ Salmonella enterica subsp. enterica serovar Typhimurium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.9
-
 ATP mutant P172T of the ATP-binding subunit HisP Salmonella enterica subsp. enterica serovar Typhimurium
1.2
-
 ATP mutant T205A of the ATP-binding subunit HisP Salmonella enterica subsp. enterica serovar Typhimurium

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane bound to Salmonella enterica subsp. enterica serovar Typhimurium 16020
-

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
-
 wild-type and mutant enzymes
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + His/out
-
 Salmonella enterica subsp. enterica serovar Typhimurium ADP + phosphate + His/in
-
 ?