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Literature summary for 3.4.21.53 extracted from

  • Goldberg, A.L.; Moerschell, R.P.; Chung, C.H.; Maurizi, M.R.
    ATP-dependent protease La (lon) from Escherichia coli (1994), Methods Enzymol., 244, 350-375.
    View publication on PubMed
Search for more literature for 3.4.21.53

Activating Compound

Activating Compound Comment Organism Structure
adenosine 5'-(3-thiotriphosphate) i.e. adenosine 5'-O-(thiotriphosphate) or ATP-gamma-S, activation Escherichia coli
adenosine 5'-(3-thiotriphosphate) not bovine serum albumin hydrolysis Escherichia coli
adenosine 5'-(3-thiotriphosphate) activates, hydrolysis of casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide Escherichia coli
Adenyl-5'-yl imidodiphosphate i.e. AMP-PNP, activation Escherichia coli
adenyl-5'-yl methylene diphosphonate i.e. AMP-PCP, activation Escherichia coli
casein ATP hydrolysis Escherichia coli
casein ATP hydrolysis Rattus norvegicus
Denatured albumin activation, ATP hydrolysis Escherichia coli
Globin ATP hydrolysis Escherichia coli
GTP activation Escherichia coli
GTP less efficient than ATP Escherichia coli
additional information enzyme hydroylzes proteins and ATP in a coupled process Brevibacillus brevis
additional information enzyme hydroylzes proteins and ATP in a coupled process Escherichia coli
additional information enzyme hydroylzes proteins and ATP in a coupled process Rattus norvegicus
additional information enzyme hydroylzes proteins and ATP in a coupled process Saccharomyces cerevisiae
additional information enzyme hydroylzes proteins and ATP in a coupled process Myxococcus xanthus
additional information nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins Brevibacillus brevis
additional information nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins Escherichia coli
additional information nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins Rattus norvegicus
additional information nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins Saccharomyces cerevisiae
additional information nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins Myxococcus xanthus
additional information no activation by ubiquitin Brevibacillus brevis
additional information no activation by ubiquitin Escherichia coli
additional information no activation by ubiquitin Rattus norvegicus
additional information no activation by ubiquitin Saccharomyces cerevisiae
additional information no activation by ubiquitin Myxococcus xanthus
additional information no activation by mRNA, tRNA, poly(rA), (dT)10 Brevibacillus brevis
additional information no activation by mRNA, tRNA, poly(rA), (dT)10 Escherichia coli
additional information no activation by mRNA, tRNA, poly(rA), (dT)10 Rattus norvegicus
additional information no activation by mRNA, tRNA, poly(rA), (dT)10 Saccharomyces cerevisiae
additional information no activation by mRNA, tRNA, poly(rA), (dT)10 Myxococcus xanthus
Poly(dT) activation Escherichia coli
Poly(rC) activation Escherichia coli
Poly(rU) activation Escherichia coli
single stranded DNA ATP and protein hydrolysis Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
3,4-dichloroisocoumarin
-
 Escherichia coli
ADP
-
 Escherichia coli
ADP
-
 Rattus norvegicus
Bacteriophage T4 protease inhibitor PinA
-
 Escherichia coli
benzyloxycarbonyl-Gly-Leu-Phe chloromethyl ketone
-
 Escherichia coli
benzyloxycarbonyl-Phe chloromethyl ketone
-
 Escherichia coli
Dansyl fluoride protein and ATP hydrolysis Escherichia coli
diisopropyl fluorophosphate
-
 Escherichia coli
diisopropyl fluorophosphate
-
 Rattus norvegicus
glycerol above 5% Escherichia coli
iodoacetamide
-
 Escherichia coli
iodoacetamide
-
 Rattus norvegicus
N-ethylmaleimide
-
 Escherichia coli
N-ethylmaleimide
-
 Rattus norvegicus
N-ethylmaleimide
-
 Saccharomyces cerevisiae
tosyl-Lys chloromethyl ketone weak, casein as substrate, no inhibition with glutaryl-Ala-Ala-Phe methoxynaphthylamide as substrate Escherichia coli
tosyl-Phe chloromethyl ketone
-
 Escherichia coli
vanadate decavanadate (not orthovanadate) Escherichia coli
vanadate
-
 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
 ATP ATP hydrolysis and protein hydrolysis, value below Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ with equal efficiency in peptide hydrolysis (not protein hydrolysis) Escherichia coli
Ca2+ less effective in caseinolysis Escherichia coli
Ca2+ poor substitute for Mg2+ in ATP hydrolysis Escherichia coli
Ca2+ activation, as Ca2+-ATP Escherichia coli
Ca2+ slight Escherichia coli
diphosphate activation Escherichia coli
Mg2+ requirement Brevibacillus brevis
Mg2+ requirement Escherichia coli
Mg2+ requirement Rattus norvegicus
Mg2+ requirement Saccharomyces cerevisiae
Mg2+ requirement Myxococcus xanthus
Mg2+ ATP hydrolysis and protease activity Brevibacillus brevis
Mg2+ ATP hydrolysis and protease activity Escherichia coli
Mg2+ ATP hydrolysis and protease activity Rattus norvegicus
Mg2+ ATP hydrolysis and protease activity Saccharomyces cerevisiae
Mg2+ ATP hydrolysis and protease activity Myxococcus xanthus
Triphosphate activation Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 E. coli enzyme behaves as apparent tetramer or octamer on gel filtration Brevibacillus brevis
additional information
-
 E. coli enzyme behaves as apparent tetramer or octamer on gel filtration Escherichia coli
additional information
-
 E. coli enzyme behaves as apparent tetramer or octamer on gel filtration Rattus norvegicus
additional information
-
 E. coli enzyme behaves as apparent tetramer or octamer on gel filtration Saccharomyces cerevisiae
additional information
-
 E. coli enzyme behaves as apparent tetramer or octamer on gel filtration Myxococcus xanthus
additional information
-
 amino acid sequence compared to other Lon-protein sequences Brevibacillus brevis
additional information
-
 amino acid sequence compared to other Lon-protein sequences Escherichia coli
additional information
-
 amino acid sequence compared to other Lon-protein sequences Rattus norvegicus
additional information
-
 amino acid sequence compared to other Lon-protein sequences Saccharomyces cerevisiae
additional information
-
 amino acid sequence compared to other Lon-protein sequences Myxococcus xanthus
88000
-
 x * 88000, calculated from nucleotide sequence Escherichia coli
94000
-
 x * 94000, SDS-PAGE Escherichia coli
800000
-
 E. coli, gel filtration Escherichia coli
840000 900000 E. coli, calculated from sedimentation coefficient and Stokes radius Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Abnormal puromucyl peptides + H2O Escherichia coli not in vitro ?
-
 ?
Canavanine-containing proteins + H2O Escherichia coli not in vitro ?
-
 ?
additional information Escherichia coli ATP-dependent serine protease ?
-
 ?
additional information Rattus norvegicus ATP-dependent serine protease ?
-
 ?
additional information Escherichia coli essential for growth of yeast on nonfermentable carbon sources ?
-
 ?
Mutant form of alkaline phosphatase PhoA61 + H2O Escherichia coli not in vitro ?
-
 ?
Proteins with highly abnormal conformation + H2O Escherichia coli one of the heat-shock proteins under control of rpoH operon(htp R) ?
-
 ?
Proteins with highly abnormal conformation + H2O Escherichia coli catalyzes inital step in the degradation of proteins with abnormal conformation as may result from nonsense or missense mutations, biosynthetic errors or intracellular denaturation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Brevibacillus brevis
-
-
-
Escherichia coli
-
-
-
Myxococcus xanthus
-
-
-
Rattus norvegicus
-
-
-
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
hydrolysis of proteins in presence of ATP hydrolysis of proteins in presence of ATP, mechanism Brevibacillus brevis
a
hydrolysis of proteins in presence of ATP hydrolysis of proteins in presence of ATP, mechanism Escherichia coli
a
hydrolysis of proteins in presence of ATP hydrolysis of proteins in presence of ATP, mechanism Rattus norvegicus
a
hydrolysis of proteins in presence of ATP hydrolysis of proteins in presence of ATP, mechanism Saccharomyces cerevisiae
a
hydrolysis of proteins in presence of ATP hydrolysis of proteins in presence of ATP, mechanism Myxococcus xanthus
a

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Saccharomyces cerevisiae
additional information
-
 0.05167 mg casein/mg enzyme/min (Escherichia coli) Escherichia coli

Storage Stability

Storage Stability Organism
-70°C, in 20-30 glycerol, many months, with prolonged storage the enzyme exhibits ATP-independent peptidase activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Abnormal puromucyl peptides + H2O not in vitro Escherichia coli ?
-
 ?
ATP + H2O
-
 Escherichia coli phosphate + ADP
-
 ?
Bacteriophage lambda protein N + H2O
-
 Escherichia coli Hydrolyzed bacteriophage lambda protein N
-
 ?
Canavanine-containing proteins + H2O not in vitro Escherichia coli ?
-
 ?
casein + H2O alpha-casein Brevibacillus brevis hydrolyzed casein
-
 ?
casein + H2O alpha-casein Escherichia coli hydrolyzed casein
-
 ?
casein + H2O alpha-casein Rattus norvegicus hydrolyzed casein
-
 ?
casein + H2O alpha-casein Saccharomyces cerevisiae hydrolyzed casein
-
 ?
casein + H2O alpha-casein Myxococcus xanthus hydrolyzed casein
-
 ?
casein + H2O methylcasein Brevibacillus brevis hydrolyzed casein
-
 ?
casein + H2O methylcasein Escherichia coli hydrolyzed casein
-
 ?
casein + H2O methylcasein Rattus norvegicus hydrolyzed casein
-
 ?
casein + H2O methylcasein Saccharomyces cerevisiae hydrolyzed casein
-
 ?
casein + H2O methylcasein Myxococcus xanthus hydrolyzed casein
-
 ?
casein + H2O beta-casein Brevibacillus brevis hydrolyzed casein
-
 ?
casein + H2O beta-casein Escherichia coli hydrolyzed casein
-
 ?
casein + H2O beta-casein Rattus norvegicus hydrolyzed casein
-
 ?
casein + H2O beta-casein Saccharomyces cerevisiae hydrolyzed casein
-
 ?
casein + H2O beta-casein Myxococcus xanthus hydrolyzed casein
-
 ?
Denatured albumin + H2O
-
 Escherichia coli ?
-
 ?
Denatured bovine serum albumin + H2O
-
 Escherichia coli ?
-
 ?
Fluorogenic peptides + H2O
-
 Escherichia coli ?
-
 ?
Globin + H2O
-
 Escherichia coli ?
-
 ?
Glucagon + H2O
-
 Escherichia coli Hydrolyzed glucagon
-
 ?
Glutaryl-Ala-Ala-Ala-methoxynaphthylamide + H2O hydrolyzed at 3-4% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide Escherichia coli Glutaryl-Ala-Ala-Ala + methoxynaphthylamine
-
 ?
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
-
 Escherichia coli Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
 ?
Glutaryl-Gly-Gly-Pro-methoxynaphthylamide + H2O hydrolyzed at 6% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide Escherichia coli Glutaryl-Gly-Gly-Pro + methoxynaphthylamine
-
 ?
additional information ATP-dependent serine protease Escherichia coli ?
-
 ?
additional information ATP-dependent serine protease Rattus norvegicus ?
-
 ?
additional information mutant enzyme in which active site Ser-679 is replaced by Ala lacks peptidase but retains ATPase activity Escherichia coli ?
-
 ?
additional information essential for growth of yeast on nonfermentable carbon sources Escherichia coli ?
-
 ?
Mutant form of alkaline phosphatase PhoA61 + H2O not in vitro Escherichia coli ?
-
 ?
Oxidized insulin B-chain + H2O cleavage sites Escherichia coli Hydrolyzed insulin B-chain
-
 ?
Proteins with highly abnormal conformation + H2O one of the heat-shock proteins under control of rpoH operon(htp R) Escherichia coli ?
-
 ?
Proteins with highly abnormal conformation + H2O catalyzes inital step in the degradation of proteins with abnormal conformation as may result from nonsense or missense mutations, biosynthetic errors or intracellular denaturation Escherichia coli ?
-
 ?
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O best substrate Escherichia coli Succinyl-Ala-Ala-Phe + methoxynaphthylamine
-
 ?
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O hydrolyzed at 137% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide Escherichia coli Succinyl-Ala-Ala-Phe + methoxynaphthylamine
-
 ?
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
-
 Escherichia coli Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
 ?
Unfolded polypeptides + H2O broad specificity Escherichia coli short peptides of 5-15 amino acids
-
 ?

Subunits

Subunits Comment Organism
multimer x * 88000, calculated from nucleotide sequence Escherichia coli
multimer x * 94000, SDS-PAGE Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
21
-
 rapid loss of activity in the absence of glycerol. ATP, AMP-PNP or ADP stabilizes, E. coli Escherichia coli
37
-
 rapid denaturation, ATP, AMP-PNP or ADP stabilizes, E. coli Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP requirement Escherichia coli
ATP two ATP molecules are hydrolyzed for each peptide bond cleaved in proteins Escherichia coli
ATP ATP-dependent protease Brevibacillus brevis
ATP ATP-dependent protease Escherichia coli
ATP ATP-dependent protease Rattus norvegicus
ATP ATP-dependent protease Saccharomyces cerevisiae
ATP ATP-dependent protease Myxococcus xanthus
ATP enzyme tetramer has high and low affinity binding sites for ATP Escherichia coli
CTP activation Escherichia coli
CTP activation Rattus norvegicus
CTP less efficient than ATP Escherichia coli
CTP less efficient than ATP Rattus norvegicus
dATP activation Escherichia coli
UTP activation Escherichia coli
UTP activation Rattus norvegicus