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Literature summary for 3.4.21.53 extracted from

  • Coleman, J.L.; Katona, L.I.; Kuhlow, C.; Toledo, A.; Okan, N.A.; Tokarz, R.; Benach, J.L.
    Evidence that two ATP-dependent (Lon) proteases in Borrelia burgdorferi serve different functions (2009), PLoS Pathog., 5, e1000676.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.53

Protein Variants

Protein Variants Comment Organism
additional information Lon-2 is able to functionally complement an Escherichia coli Lon mutant Borreliella burgdorferi
S714A mutation of the predicted catalytic site serine residue. Mutant does not show catalytic activity. In presence of ATP, mutant exhibits a chaperone-like activity by inhibiting the aggregation of insulin beta-chain Borreliella burgdorferi

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Borreliella burgdorferi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
90700
-
 x * 90700, calculated and SDS-PAGE Borreliella burgdorferi

Organism

Organism UniProt Comment Textmining
Borreliella burgdorferi O51558 isoform Lon-2
-
Borreliella burgdorferi Q59185 isoform Lon-1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-casein-fluorescein isothiocyanate + H2O
-
 Borreliella burgdorferi ?
-
 ?
beta-galactosidase + H2O
-
 Borreliella burgdorferi ?
-
 ?
additional information the ATPase and the proteolytic domains function independently. Introduction of a mutation into the proteolytic domain does not affect the ability of Lon-1 to hydrolyze ATP. Lon-1 does not degrade Borrelia-SsrA tagged reporter protein in vitro Borreliella burgdorferi ?
-
 ?
SulA + H2O i.e. cell division inhibitor Borreliella burgdorferi ?
-
 ?

Subunits

Subunits Comment Organism
? x * 90700, calculated and SDS-PAGE Borreliella burgdorferi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 9.5
-
 Borreliella burgdorferi

General Information

General Information Comment Organism
physiological function Lon-1 may be important in host adaptation from the arthropod to a warm-blooded host. Recombinant Lon-1 shows properties of an ATP-dependent chaperone protease in vitro but does not complement an Escherichia coli Lon mutant Borreliella burgdorferi
physiological function Lon-2 is engaged in cellular homeostasis Borreliella burgdorferi