| magnesium-importing ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a Mg2+-importing ATPase (EC 3.6.3.2) is an enzyme that catalyzes the chemical reaction
- ATP + H2O + Mg2+out ADP + phosphate + Mg2+in
The 3 substrates of this enzyme are ATP, H2O, and Mg2+, whereas its 3 products are ADP, phosphate, and Mg2+.
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 (Mg2+-importing).
The mgtA gene which encodes this enzyme is thought to be regulated by a magnesium responsive RNA element.[1] A human enzyme was found in erythrocytes[2] but the observation could not be confirmed.
References
- ↑ 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. PMID 17381304.
- ↑ 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. PMID 15820777.
- 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. PMC 176934. PMID 7751273.
- 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. PMID 9786860.
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