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Literature summary extracted from

  • Mertova, J.; Almasiova, M.; Perecko, D.; Bilka, F.; Benesova, M.; Bezakova, L.; Psenak, M.; Kutejova, E.
    ATP-dependent Lon protease from maize mitochondria - comparison with the other Lon proteases (2002), Biologia, 57, 739-745.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.53 ATP enzyme needs ATP for its activity and stability. Properties compared with ATP-dependent proteases from different sources Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.53 ADP 2 mM Zea mays
3.4.21.53 diisopropyl fluorophosphate
-
 Zea mays
3.4.21.53 ethylenediaminetetraacetic acid
-
 Zea mays
3.4.21.53 iodoacetamide
-
 Zea mays
3.4.21.53 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
3.4.21.53 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
3.4.21.53 phenylmethylsulfonyl fluoride
-
 Zea mays
3.4.21.53 vanadate
-
 Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.53 mitochondrion prepared from 4days old epicotyls of Zea mays L. seedlings Zea mays 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.53 Mg2+ enzyme needs Mg2+ ions for its activity and stability. Properties compared with ATP-dependent proteases from different sources Zea mays

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.53 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
3.4.21.53 977000
-
 predicted molecular mass of the subunit calculated from the gene Zea mays

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.53 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.53 139fold, ion exchange chromatography and gel filtration Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.53 epicotyl
-
 Zea mays
-

Storage Stability

EC Number Storage Stability Organism
3.4.21.53 High protease instability is caused by its degradation during storage of mitochondria at -70°C as well as during the isolation. Zea mays

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.53 casein + H2O
-
 Zea mays ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.53 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

EC Number Synonyms Comment Organism
3.4.21.53 lon
-
 Zea mays
3.4.21.53 lon protease endoprotease Zea mays
3.4.21.53 serine protease
-
 Zea mays

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.53 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.53 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 Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.53 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