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Literature summary for 3.4.21.53 extracted from

  • Stahlberg, H.; Kutejova, E.; Suda, K.; Wolpensinger, B.; Lustig, A.; Schatz, G.; Engel, A.; Suzuki, C.K.
    Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits (1999), Proc. Natl. Acad. Sci. USA, 96, 6787-6790.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.53

Activating Compound

Activating Compound Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae

General Stability

General Stability Organism
The pure active lon is unstable at 30°C, presumably because it cleaves itself, but degradation is prevented by 1 mM ATP or AMP-PNP. These nucleotides stabilize both the individual subunits as well as the oligomeric enzyme, suggesting that stabilization required binding but not hydrolysis of ATP. Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Saccharomyces cerevisiae 5739
-
soluble
-
 Saccharomyces cerevisiae
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
117000
-
 each lon subunit has a mass of 117 kDa, heptamer Saccharomyces cerevisiae
804000
-
 scanning transmission electron microscopy mass analysis Saccharomyces cerevisiae
804000
-
 scanning Transmission Electron Microscopy (STEM) Mass Analysis. To determine the number of subunits in the holoenzyme, the mass of pure, active lon is measured by STEM. When lon purified in the presence of ATP is crosslinked with 0.1% glutaraldehyde, adsorbed onto thin carbon film, freeze-dried, and imaged in the STEM, circular particles of uniform brightness are seen. The measured mass values have a Gaussian distribution with a single peak at 804 kDa Saccharomyces cerevisiae
818000
-
 analytical ultracentrifugation Saccharomyces cerevisiae
818000
-
 measuring the mass of the pure enzyme complex by analytical ultracentrifugation. When purified in the presence of ATP, enzyme has a mass of 818 kDa as determined by sedimentation velocity. Adding ATP is essential for preserving the Lon oligomer during ultracentrifugation Saccharomyces cerevisiae
838000
-
 measuring the mass of the pure enzyme complex by analytical ultracentrifugation. When purified in the presence of ATP, enzyme has a mass of 838 kDa as determined by sedimentation to equilibrium. Adding ATP is essential for preserving the Lon oligomer during ultracentrifugation Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae
-
 yeast
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae
active lon carrying six C-terminal histidine residues is overexpressed in yeast, is rapidly purified to homogeneity from an isolated mitochondrial extract on a Ni21-NTA column, and purified to homogeneity by gel filtration on a Superose 6 column Saccharomyces cerevisiae

Subunits

Subunits Comment Organism
heptamer 7 * 117000, SDS-PAGE Saccharomyces cerevisiae
heptamer ring-shaped protease with seven flexible subunits, ultracentrifugation thus showed lon to be a heptamer, in excellent agreement with the STEM analysis Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
la
-
 Saccharomyces cerevisiae
lon
-
 Saccharomyces cerevisiae
lon (Pim1p) protease
-
 Saccharomyces cerevisiae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
 pure active Lon is unstable at 30°C Saccharomyces cerevisiae
30
-
 the pure active lon is unstable at 30°C, presumably because it cleaves itself, but degradation is prevented by 1 mM ATP or AMP-PNP. These nucleotides stabilize both the individual subunits as well as the oligomeric enzyme, suggesting that stabilization required binding but not hydrolysis of ATP Saccharomyces cerevisiae