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Literature summary extracted from
- Probing structure-function relationships and gating mechanisms in the CorA Mg2+ transport system (2008), J. Biol. Chem., 283, 11721-11733.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 7.2.2.14 | expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21, complementation of Salmonella typhimurium MM281, a strain devoid of all genomic Mg2+ transport systems | Thermotoga maritima |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 7.2.2.14 | D253F | site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
| 7.2.2.14 | D253K | site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
| 7.2.2.14 | D253W | site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
| 7.2.2.14 | E206R | site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
| 7.2.2.14 | E316K | site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
| 7.2.2.14 | E316K/E320A | site-directed mutagenesis, with mutation of Gly4alpha5alpha6, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
| 7.2.2.14 | E320K | site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
| 7.2.2.14 | additional information | deletion mutant Gly4alpha5alpha6, site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
| 7.2.2.14 | P303I | site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
| 7.2.2.14 | V194E | site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
| 7.2.2.14 | V194E/E206R | site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview | Thermotoga maritima |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.2.2.14 | membrane | - |
Thermotoga maritima | 16020 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.2.2.14 | ATP + H2O + Mg2+/out | Thermotoga maritima | - |
ADP + phosphate + Mg2+/in | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.2.2.14 | Thermotoga maritima | Q9WZ31 | gene corA | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.2.2.14 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography, cleavage of the His-tag, and gel filtration to homogeneity | Thermotoga maritima |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 7.2.2.14 | reconstitution of the purified recombinant enzyme in phosphatidylcholine liposomes, overview | Thermotoga maritima |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.2.2.14 | ATP + H2O + Mg2+/out | - |
Thermotoga maritima | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | ATP + H2O + Mg2+/out | CorA contains an unusually long ion pore putatively gated by hydrophobic residues near the intracellular end and by universally conserved asparagine residues at the periplasmic entrance, structure-function relationships and gating mechanisms in the CorA Mg2+ transport system, the intracellular funnel domain constitutes an allosteric regulatory module that can be engineered to promote an activated or closed state, involvement of the alpha5 and alpha6 helices in CorA function, overview | Thermotoga maritima | ADP + phosphate + Mg2+/in | - |
? | |
| 7.2.2.14 | additional information | CorA is selective for magnesium ions over calcium ions with a 100fold greater uptake rate | Thermotoga maritima | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.2.2.14 | More | CorA contains an unusually long ion pore putatively gated by hydrophobic residues near the intracellular end and by universally conserved asparagine residues at the periplasmic entrance | Thermotoga maritima |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.2.2.14 | CorA | - |
Thermotoga maritima |
| 7.2.2.14 | More | the enzyme belongs to the CorA-Alr1-Mrs2 superfamily | Thermotoga maritima |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.14 | 25 | - |
assay at | Thermotoga maritima |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.2.2.14 | 7.2 | - |
assay at | Thermotoga maritima |
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Release 2023.1 (January 2023)
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