Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Synechocystis sp. |
Protein Variants | Comment | Organism |
---|---|---|
E152Q | mutation in the AAA+ domain of ChlD binds to ChlI. Mutant shows low activity but assembles into complexes much like wild-type. Mutant shows 25% of wild-type activity. kcat/K0.5 for Mg2+ is 30% of wild-type. kcat and Km for deuteroporphyrin are reduced to the same extent | Synechocystis sp. |
K49A | mutation in the AAA+ domain of ChlD binds to ChlI. Mutant shows no activity. Mutant forms detecable amount of ChlID complexes | Synechocystis sp. |
R208A | mutation in the AAA+ domain of ChlD binds to ChlI. Mutant shows reduced binding affinity to ChlI.Mutant shows 50% of wild-type activity (least impaired mutant). Effect on substrate handling is modest compared to wild-type. Specifictiy constants for Mg2+ and porphyrin are 70% of wild-type | Synechocystis sp. |
R289A | mutation in the AAA+ domain of ChlD binds to ChlI. Mutant shows reduced binding affinity to ChlI. Mutant shows 13% of wild-type activity. Mutant does not show a cooperative response to MgATP2- and has much weaker specificity toward Mg2+ than wild-type. Mutant has a lower specificity toward free porphyrin than wild-type | Synechocystis sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00099 | - |
deuteroporphyrin | mutant R289A, pH 7.7, 34°C | Synechocystis sp. | |
0.0012 | - |
deuteroporphyrin | mutant E152Q, pH 7.7, 34°C | Synechocystis sp. | |
0.0057 | - |
deuteroporphyrin | wild-type, pH 7.7, 34°C | Synechocystis sp. | |
0.00631 | - |
deuteroporphyrin | mutant R208A, pH 7.7, 34°C | Synechocystis sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. | - |
- |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography | Synechocystis sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + deuteroporphyrin + Mg2+ + H2O | - |
Synechocystis sp. | ADP + phosphate + Mg-deuteroporphyrin + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
magnesium chelatase | - |
Synechocystis sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
34 | - |
assay at | Synechocystis sp. |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0009 | - |
ATP | mutant R289A, pH 7.7, 34°C | Synechocystis sp. | |
0.0013 | - |
deuteroporphyrin | mutant R289A, pH 7.7, 34°C | Synechocystis sp. | |
0.0018 | - |
ATP | mutant E152Q, pH 7.7, 34°C | Synechocystis sp. | |
0.0028 | - |
Mg2+ | mutant E152Q, pH 7.7, 34°C | Synechocystis sp. | |
0.003 | - |
deuteroporphyrin | mutant E152Q, pH 7.7, 34°C | Synechocystis sp. | |
0.0043 | - |
ATP | mutant R208A, pH 7.7, 34°C | Synechocystis sp. | |
0.0067 | - |
ATP | wild-type, pH 7.7, 34°C | Synechocystis sp. | |
0.0081 | - |
Mg2+ | wild-type, pH 7.7, 34°C | Synechocystis sp. | |
0.0083 | - |
Mg2+ | mutant R208A, pH 7.7, 34°C | Synechocystis sp. | |
0.014 | - |
deuteroporphyrin | mutant R208A, pH 7.7, 34°C | Synechocystis sp. | |
0.0188 | - |
deuteroporphyrin | wild-type, pH 7.7, 34°C | Synechocystis sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.7 | - |
assay at | Synechocystis sp. |