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Information on EC 3.4.21.53 - Endopeptidase La and Organism(s) Borreliella burgdorferi and UniProt Accession O51558

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.53 Endopeptidase La
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This record set is specific for:
Borreliella burgdorferi
UNIPROT: O51558 not found.
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Word Map
The taxonomic range for the selected organisms is: Borreliella burgdorferi
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hydrolysis of proteins in presence of ATP
Synonyms
protease, serine protease, clpxp, lon protease, lonp1, protease la, atp-dependent lon protease, protease lon, aaa+ protease, ms-lon, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP-dependent Lon proteinase
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ATP-dependent protease La
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ATP-dependent serine proteinase
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Escherichia coli proteinase La
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Escherichia coli serine proteinase La
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Gene lon protease
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Gene lon proteins
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Lon proteinase
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PIM1 protease
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PIM1 proteinase
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Protease La
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Proteinase La
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Proteinase, Escherichia coli serine, La
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Proteinase, La
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Proteins, gene lon
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Proteins, specific or class, gene lon
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Serine protease La
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CAS REGISTRY NUMBER
COMMENTARY hide
79818-35-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-casein-fluorescein isothiocyanate + H2O
?
show the reaction diagram
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-
-
?
beta-galactosidase + H2O
?
show the reaction diagram
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?
SulA + H2O
?
show the reaction diagram
i.e. cell division inhibitor
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-
?
alpha-casein-fluorescein isothiocyanate + H2O
?
show the reaction diagram
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-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform Lon-2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Lon-2 is engaged in cellular homeostasis
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90700
x * 90700, calculated and SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 90700, calculated and SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
PLoS Pathog.
5
e1000676
2009
Borreliella burgdorferi (O51558), Borreliella burgdorferi (Q59185), Borreliella burgdorferi
Manually annotated by BRENDA team