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Literature summary extracted from

  • Suzuki, C.K.; Kutejova, E.; Suda, K.
    Analysis and purification of ATP-dependent mitochondrial lon protease of Saccharomyces cerevisiae (1995), Methods Enzymol., 260, 486-494.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.53 ATP
-
 Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.53 diisopropyl fluorophosphate inhibition indicates that the enzyme is a serine protease Saccharomyces cerevisiae
3.4.21.53 N-ethylmaleimide
-
 Escherichia coli
3.4.21.53 N-ethylmaleimide enzyme particularly sensitive to, pointing to an essential role of sulfllydryl groups in enzymatic activity Saccharomyces cerevisiae
3.4.21.53 phenylmethylsulfonyl fluoride inhibition indicates that the enzyme is a serine protease Saccharomyces cerevisiae
3.4.21.53 PMSF
-
 Escherichia coli
3.4.21.53 PMSF
-
 Saccharomyces cerevisiae
3.4.21.53 vanadate
-
 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.53 mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.53 additional information
-
 amino acid sequence compared to other Lon-protein sequences Escherichia coli
3.4.21.53 additional information
-
 amino acid sequence compared to other Lon-protein sequences Saccharomyces cerevisiae
3.4.21.53 106000
-
 6 * 106000, human, calculated from amino acid sequence Escherichia coli
3.4.21.53 106000
-
 6 * 106000, human, calculated from amino acid sequence Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.53 additional information Escherichia coli
-
 ?
-
 ?
3.4.21.53 additional information Saccharomyces cerevisiae involved in mitochondrial protein turnover ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.53 Escherichia coli
-
-
-
3.4.21.53 Saccharomyces cerevisiae
-
-
-
3.4.21.53 Saccharomyces cerevisiae
-
 yeast, mutant strain pep949
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.53 protein purification procedure utilizes mitochondria from the mutant strain pep949 (MATa/alpha, prl 1-1122, prc 1-40Z, pep 4-3, leu2, trp 1, ura 3-52) Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.53 casein + H2O alpha-casein Escherichia coli hydrolyzed casein
-
 ?
3.4.21.53 casein + H2O alpha-casein Saccharomyces cerevisiae hydrolyzed casein
-
 ?
3.4.21.53 casein + H2O alpha-casein (alpha1-casein) Saccharomyces cerevisiae hydrolyzed casein
-
 ?
3.4.21.53 additional information
-
 Escherichia coli ?
-
 ?
3.4.21.53 additional information involved in mitochondrial protein turnover Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.53 hexamer 6 * 106000, human, calculated from amino acid sequence Escherichia coli
3.4.21.53 hexamer 6 * 106000, human, calculated from amino acid sequence Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
3.4.21.53 lon protease
-
 Saccharomyces cerevisiae
3.4.21.53 protease
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.53 37
-
 assay at Escherichia coli
3.4.21.53 37
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.21.53 ATP ATP-dependent protease Escherichia coli
3.4.21.53 ATP ATP-dependent protease Saccharomyces cerevisiae