Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | enzyme needs ATP for its activity and stability. Properties compared with ATP-dependent proteases from different sources | Zea mays |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | 2 mM | Zea mays | |
diisopropyl fluorophosphate | - |
Zea mays | |
ethylenediaminetetraacetic acid | - |
Zea mays | |
iodoacetamide | - |
Zea mays | |
additional information | inhibitory profile corresponds to those of ATP-dependent serine proteases of Lon (La) family. Properties compared with ATP-dependent proteases from different sources | Zea mays | |
N-ethylmaleimide | the candidate for the NEM binding could be Cys406 located close to the ATP binding site (Gly409-Ser417) and highly conserved between Lon proteases | Zea mays | |
phenylmethylsulfonyl fluoride | - |
Zea mays | |
vanadate | - |
Zea mays |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | prepared from 4days old epicotyls of Zea mays L. seedlings | Zea mays | 5739 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | enzyme needs Mg2+ ions for its activity and stability. Properties compared with ATP-dependent proteases from different sources | Zea mays |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
700000 | - |
molecular mass of the isolated enzyme determined by gel filtration is about 700 kDa. Properties compared with ATP-dependent proteases from different sources | Zea mays |
977000 | - |
predicted molecular mass of the subunit calculated from the gene | Zea mays |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | - |
- |
- |
Purification (Comment) | Organism |
---|---|
139fold, ion exchange chromatography and gel filtration | Zea mays |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
epicotyl | - |
Zea mays | - |
Storage Stability | Organism |
---|---|
High protease instability is caused by its degradation during storage of mitochondria at -70°C as well as during the isolation. | Zea mays |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
casein + H2O | - |
Zea mays | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
heptamer | maize Lon can form a heptameric ring similar to that of yeast Lon. Enzyme with considerably less stability than other mitochondrial Lon proteases. Properties compared with ATP-dependent proteases from different sources | Zea mays |
Synonyms | Comment | Organism |
---|---|---|
lon | - |
Zea mays |
lon protease | endoprotease | Zea mays |
serine protease | - |
Zea mays |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | 45 | optimal pH is 8.5-9.0 and optimal temperature 40-45°C, suggesting the heat shock character of the enzyme. Properties compared with ATP-dependent proteases from different sources | Zea mays |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | 9 | optimal pH is 8.5-9.0 and optimal temperature 40-45°C, suggesting the heat shock character of the enzyme. Properties compared with ATP-dependent proteases from different sources show similarity to the optimum of the other Lon proteases | Zea mays |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 9.5 | influence of pH to enzyme activity is determined using MES buffer for pH 6.0-7.0, MOPS buffer for pH 6.5-8.0 and glycine buffer for pH 8.5-9.5 | Zea mays |