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Literature summary extracted from

  • Makhovskaya, O.V.; Kozlov, S.; Botos, I.; Stepnov, A.A.; Andrianova, A.G.; Gushchina, A.E.; Wlodawer, A.; Melnikov, E.E.; Rotanova, T.V.
    Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: the contribution of the quaternary structure to the regulation of enzyme proteolytic activity (2007), Russ. J. Bioorg. Chem., 33, 610-613.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.53
-
 Archaeoglobus fulgidus
3.4.21.53 mutants cloned into vector pET24a(+), expressed in Escherichia coli Rosetta (DE3) pLysS Archaeoglobus fulgidus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.53 deltaTM(1)-lon-S509A possesses neither proteolytic nor ATPase activity, is completely stable, can be considered as model of initial active delta TM(1)-lon forms Archaeoglobus fulgidus
3.4.21.53 deltaTM(2)-lon-S509A possesses neither proteolytic nor ATPase activity, is completely stable, can be considered as model of initial active delta TM(2)-lon forms Archaeoglobus fulgidus
3.4.21.53 deltaTM1-lon deletion of 100-186, leads to the removal of the predicted hydrophobic site of the transmembrane domain Archaeoglobus fulgidus
3.4.21.53 deltaTM2-lon deletion of 119-222, leads to the removal of the predicted hydrophobic site of the transmembrane domain Archaeoglobus fulgidus
3.4.21.53 additional information deletion of the transmembrane domain results in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both alpha-helical and proteolytic domains Archaeoglobus fulgidus
3.4.21.53 additional information deletion of the transmembrane domain of LonB protease results in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both alpha-helical and proteolytic domains. The enzyme form with a transmembrane deletion and an additional site-directed mutagenesis at S509A (the catalytic Ser residue), is capable of recombination with the proteolytic-domain fragment. The mixed oligomers are proteolytically active, which indicates a crucial role of subunit interactions in the activation of the proteolytic site Archaeoglobus fulgidus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.53 36000
-
 mutants deltaTM1-lon and deltaTM2-lon Archaeoglobus fulgidus
3.4.21.53 68200
-
 x * 68200, the subunit consist of ATPase and proteolytic domains Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.53 Archaeoglobus fulgidus
-
-
-
3.4.21.53 Archaeoglobus fulgidus O29883
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.53 ATP + H2O oligomeric organization of lon protease and ATP hydrolysis are necessary prerequisites of realization of the processive degradation of a protein substrate Archaeoglobus fulgidus phosphate + ADP
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.53 oligomer x * 68200, the subunit consist of ATPase and proteolytic domains Archaeoglobus fulgidus

Synonyms

EC Number Synonyms Comment Organism
3.4.21.53 AfLon
-
 Archaeoglobus fulgidus
3.4.21.53 ATP-dependent lon protease
-
 Archaeoglobus fulgidus
3.4.21.53 lonB protease
-
 Archaeoglobus fulgidus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.53 70
-
-
 Archaeoglobus fulgidus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.53 additional information
-
 thermophilic nature of lon protease is due to special features of enzyme activity regulation, structure of ATPase domain, and quaternary structure Archaeoglobus fulgidus
3.4.21.53 additional information
-
 the thermophilic nature of Lon protease is due to the special features of the enzyme activity regulation, the structure of ATPase domain, and the quaternary structure Archaeoglobus fulgidus