View source for Mg2+-importing ATPase

{{Short description|Class of enzymes}}
{{infobox enzyme
| Name       = magnesium-importing ATPase
| EC_number  = 3.6.3.2
| CAS_number =
| GO_code    = 0015444
| image      = 
| width      = 
| caption    =  
}}
In [[enzymology]], a '''Mg<sup>2+</sup>-importing ATPase''' ({{EC number|3.6.3.2}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:ATP + H<sub>2</sub>O + Mg<sub>2</sub>+out <math>\rightleftharpoons</math> ADP + phosphate + Mg<sub>2</sub>+in

The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]], [[water|H<sub>2</sub>O]], and [[magnesium|Mg<sup>2+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]], [[phosphate]], and Mg<sup>2+</sup>.

This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The [[List of enzymes|systematic name]] of this enzyme class is '''ATP phosphohydrolase (Mg<sup>2+</sup>-importing)'''.

The ''mgtA'' gene which encodes this enzyme is thought to be regulated by a [[magnesium responsive RNA element]].<ref name="pmid17381304">{{cite journal |vauthors=Groisman EA, Cromie MJ, Shi Y, Latifi T |title=A Mg2+-responding RNA that controls the expression of a Mg2+ transporter. |journal=Cold Spring Harb Symp Quant Biol |volume=71 |pages=251–8 |year=2006 |pmid=17381304 |doi=10.1101/sqb.2006.71.005|doi-access=free }}</ref> A human enzyme was found in [[erythrocytes]]<ref name="pmid15820777">{{cite journal |vauthors=Szemraj J, Sobolewska B, Gulczynska E, Wilczynski J, Zylinska L |title=Magnesium sulfate effect on erythrocyte membranes of asphyxiated newborns |journal=Clin. Biochem. |volume=38 |issue=5 |pages=457–64 |date=May 2005 |pmid=15820777 |doi=10.1016/j.clinbiochem.2005.02.005 }}</ref> but the observation could not be confirmed.

==References==
{{reflist|1}}
{{refbegin}}
:* {{cite journal | vauthors = Tao T, Snavely MD, Farr SG, Maguire ME | year = 1995 | title = 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 | journal = J. Bacteriol.  | volume = 177 | pages = 2654&ndash;62  | pmid = 7751273 | issue = 10 | pmc = 176934 | doi=10.1128/jb.177.10.2654-2662.1995}}
:* {{cite journal | vauthors = Kaczmarek MT, Maguire ME | year = 1998 | title = The CorA Mg2+ transport protein of Salmonella typhimurium Mutagenesis of conserved residues in the third membrane domain identifies a Mg2+ pore | journal = J. Biol. Chem.  | volume = 273 | pages = 28663&ndash;9  | pmid = 9786860 | doi = 10.1074/jbc.273.44.28663 | issue = 44 | doi-access = free }}
{{refend}}

{{Acid anhydride hydrolases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}

[[Category:EC 3.6.3]]
[[Category:Enzymes of unknown structure]]


{{3.6-enzyme-stub}}