Mg2+-importing ATPase
Appearance
(Redirected fromATP3)
magnesium-importing ATPase | |||||||||
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Identifiers | |||||||||
EC no. | 3.6.3.2 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDBstructures | RCSB PDBPDBePDBsum | ||||||||
Gene Ontology | AmiGO/QuickGO | ||||||||
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Inenzymology,aMg2+-importing ATPase(EC3.6.3.2) is anenzymethatcatalyzesthechemical reaction
- ATP + H2O + Mg2+outADP + phosphate + Mg2+in
The 3substratesof this enzyme areATP,H2O,andMg2+,whereas its 3productsareADP,phosphate,and Mg2+.
This enzyme belongs to the family ofhydrolases,specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. Thesystematic nameof this enzyme class isATP phosphohydrolase (Mg2+-importing).
ThemgtAgene which encodes this enzyme is thought to be regulated by amagnesium responsive RNA element.[1]A human enzyme was found inerythrocytes[2]but the observation could not be confirmed.
References
[edit]- ^Groisman EA, Cromie MJ, Shi Y, Latifi T (2006)."A Mg2+-responding RNA that controls the expression of a Mg2+ transporter".Cold Spring Harb Symp Quant Biol.71:251–8.doi:10.1101/sqb.2006.71.005.PMID17381304.
- ^Szemraj J, Sobolewska B, Gulczynska E, Wilczynski J, Zylinska L (May 2005). "Magnesium sulfate effect on erythrocyte membranes of asphyxiated newborns".Clin. Biochem.38(5): 457–64.doi:10.1016/j.clinbiochem.2005.02.005.PMID15820777.
- Tao T, Snavely MD, Farr SG, Maguire ME (1995)."Magnesium transport in Salmonella typhimurium: mgtA encodes a P-type ATPase and is regulated by Mg2+ in a manner similar to that of the mgtB P-type ATPase".J. Bacteriol.177(10): 2654–62.doi:10.1128/jb.177.10.2654-2662.1995.PMC176934.PMID7751273.
- Kaczmarek MT, Maguire ME (1998)."The CorA Mg2+ transport protein of Salmonella typhimurium Mutagenesis of conserved residues in the third membrane domain identifies a Mg2+ pore".J. Biol. Chem.273(44): 28663–9.doi:10.1074/jbc.273.44.28663.PMID9786860.