Polar-amino-acid-transporting ATPase

polar-amino acid-transporting ATPase
Identifiers
EC number 3.6.3.21
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a polar-amino-acid-transporting ATPase (EC 3.6.3.21) is an enzyme that catalyzes the chemical reaction

ATP + H2O + polar amino acidout ⇌ ADP + phosphate + polar amino acidin

The 3 substrates of this enzyme are ATP, H2O, and polar amino acid, whereas its 3 products are ADP, phosphate, and polar amino acid.

This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (polar-amino-acid-importing). This enzyme is also called histidine permease. This enzyme participates in abc transporters - general.

References

    • Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH (1995). "Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases". Res. Microbiol. 146 (4): 271&ndash, 8. doi:10.1016/0923-2508(96)81050-3. PMID 7569321.
    • Saier MH Jr (1998). "Advances in Microbial Physiology Volume 40". Adv. Microb. Physiol. Advances in Microbial Physiology. 40: 81&ndash, 136. doi:10.1016/S0065-2911(08)60130-7. ISBN 978-0-12-027740-7. PMID 9889977. |chapter= ignored (help)
    • Nikaido K, Liu PQ, Ames GF (1997). "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. 272 (44): 27745&ndash, 52. doi:10.1074/jbc.272.44.27745. PMID 9346917.
    • Walshaw DL, Lowthorpe S, East A, Poole PS (1997). "Distribution of a sub-class of bacterial ABC polar amino acid transporter and identification of an N-terminal region involved in solute specificity". FEBS Lett. 414 (2): 397&ndash, 401. doi:10.1016/S0014-5793(97)01023-5. PMID 9315727.


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