Literature summary extracted from
Davison, P.A.; Hunter, C.N.
Abolition of magnesium chelatase activity by the gun5 mutation and reversal by Gun4 (2011), FEBS Lett., 585, 183-186.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
6.6.1.1 |
Gun4 |
addition of Gun4 up to 0.0005 mM stimulates the wild type enzyme 2-3fold. Up to 0.001 mM Gun4 resurrects the inactive gun5 and cch mutant Mg-chelatase reactions to the level seen in the wild type with no Gun4 present, particularly in the case of mutant gun5 |
Synechocystis sp. |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
6.6.1.1 |
mutant enzymes are expressed in Escherichia coli |
Synechocystis sp. |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
6.6.1.1 |
A942V |
the (gun5) mutation abolishes activity of Mg-chelatase subunit H. Increasing the ChlH concentration up to 0.02 mM restores approximately 50% activity in the presence of the gun5 mutation. The addition of Gun4 restores Mg-chelatase activity of the gun5 mutant enzyme |
Synechocystis sp. |
6.6.1.1 |
P595L |
the (cch) mutation abolishes activity of Mg-chelatase subunit H. Increasing the ChlH concentration up to 0.02 mM fully restores activity in the presence of the cch mutation. The addition of Gun4 restores Mg-chelatase activity of the cch mutant enzyme |
Synechocystis sp. |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
6.6.1.1 |
Mg2+ |
required |
Synechocystis sp. |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
6.6.1.1 |
39000 |
- |
1 * 148000 + 1 * 39000 + 1 * 73000, subunits ChlH, ChlI and ChlD |
Synechocystis sp. |
6.6.1.1 |
73000 |
- |
1 * 148000 + 1 * 39000 + 1 * 73000, subunits ChlH, ChlI and ChlD |
Synechocystis sp. |
6.6.1.1 |
148000 |
- |
1 * 148000 + 1 * 39000 + 1 * 73000, subunits ChlH, ChlI and ChlD |
Synechocystis sp. |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
6.6.1.1 |
Synechocystis sp. |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
6.6.1.1 |
mutant enzymes are purified by Ni2+ affinity column chromatography |
Synechocystis sp. |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
6.6.1.1 |
ATP + protoporphyrin IX + Mg2+ + H2O |
- |
Synechocystis sp. |
ADP + phosphate + Mg-protoporphyrin IX + H+ |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
6.6.1.1 |
heterotrimer |
1 * 148000 + 1 * 39000 + 1 * 73000, subunits ChlH, ChlI and ChlD |
Synechocystis sp. |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
6.6.1.1 |
ChlH |
subunit of the magnesium chelatase |
Synechocystis sp. |
6.6.1.1 |
ChlHID |
- |
Synechocystis sp. |
6.6.1.1 |
Mg-chelatase |
- |
Synechocystis sp. |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
6.6.1.1 |
metabolism |
magnesium chelatase catalyses the first committed step of chlorophyll biosynthesis |
Synechocystis sp. |