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 | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.05 | - |
ATP | ATP hydrolysis and protein hydrolysis, value below | Escherichia coli |
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 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Brevibacillus brevis | - |
- |
- |
Escherichia coli | - |
- |
- |
Myxococcus xanthus | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
hydrolysis of proteins in presence of ATP | hydrolysis of proteins in presence of ATP, mechanism | Brevibacillus brevis | |
hydrolysis of proteins in presence of ATP | hydrolysis of proteins in presence of ATP, mechanism | Escherichia coli | |
hydrolysis of proteins in presence of ATP | hydrolysis of proteins in presence of ATP, mechanism | Rattus norvegicus | |
hydrolysis of proteins in presence of ATP | hydrolysis of proteins in presence of ATP, mechanism | Saccharomyces cerevisiae | |
hydrolysis of proteins in presence of ATP | hydrolysis of proteins in presence of ATP, mechanism | Myxococcus xanthus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Rattus norvegicus | - |
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 | Organism |
---|---|
-70°C, in 20-30 glycerol, many months, with prolonged storage the enzyme exhibits ATP-independent peptidase activity | Escherichia coli |
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 | Comment | Organism |
---|---|---|
multimer | x * 88000, calculated from nucleotide sequence | Escherichia coli |
multimer | x * 94000, SDS-PAGE | Escherichia coli |
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 | 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 |