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Literature summary for 3.4.21.53 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)

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

Protein Variants

Protein Variants Comment Organism
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
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
deltaTM1-lon deletion of 100-186, leads to the removal of the predicted hydrophobic site of the transmembrane domain Archaeoglobus fulgidus
deltaTM2-lon deletion of 119-222, leads to the removal of the predicted hydrophobic site of the transmembrane domain Archaeoglobus fulgidus
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
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]

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

Organism

Organism UniProt Comment Textmining
Archaeoglobus fulgidus
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-
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Archaeoglobus fulgidus O29883
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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