Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.53 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
Search for more literature for 3.4.21.53

Activating Compound

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

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

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

Metals/Ions

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 [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

Organism UniProt Comment Textmining
Zea mays
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
epicotyl
-
 Zea mays
-

Storage Stability

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 and Products (Substrate)

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

Subunits

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

Synonyms Comment Organism
lon
-
 Zea mays
lon protease endoprotease Zea mays
serine protease
-
 Zea mays

Temperature Optimum [°C]

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

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 Range

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