EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.53 | adenosine 5'-(3-thiotriphosphate) | i.e. adenosine 5'-O-(thiotriphosphate) or ATP-gamma-S, activation | Escherichia coli | |
3.4.21.53 | adenosine 5'-(3-thiotriphosphate) | hydrolysis, peptide not protein hydrolysis | Escherichia coli | |
3.4.21.53 | Adenyl-5'-yl imidodiphosphate | casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis | Escherichia coli | |
3.4.21.53 | Adenyl-5'-yl imidodiphosphate | no activation of bovine serum albumin hydrolysis | Escherichia coli | |
3.4.21.53 | adenyl-5'-yl methylene diphosphonate | i.e. AMP-PCP, activation | Escherichia coli | |
3.4.21.53 | adenyl-5'-yl methylene diphosphonate | casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis | Escherichia coli | |
3.4.21.53 | GTP | activation | Escherichia coli | |
3.4.21.53 | GTP | less efficient than ATP | Escherichia coli | |
3.4.21.53 | additional information | enzyme hydroylzes proteins and ATP in a coupled process | Escherichia coli | |
3.4.21.53 | additional information | peptide substrates, e.g. glutaryl-Ala-Phe-Phe methoxynaphthylamide or succinyl-Phe-Leu-Phe methoxynaphthylamide do not support ATP hydrolysis | Escherichia coli | |
3.4.21.53 | additional information | polyphosphate (n:17) | Escherichia coli | |
3.4.21.53 | additional information | protein degradation requires nucleoside triphosphate hydrolysis, cleavage of small peptides only requires binding of nucleotides to the enzyme | Escherichia coli | |
3.4.21.53 | Protein substrates | promotion of ATP hydrolysis | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.53 | ADP | prevents activation by ATP; prevents activation by diphosphate | Escherichia coli | |
3.4.21.53 | Glutaryl-Ala-Ala-Phe | ATP hydrolysis | Escherichia coli | |
3.4.21.53 | Glutaryl-Ala-Ala-Phe-methoxynaphthylamide | ATP-hydrolysis | Escherichia coli | |
3.4.21.53 | Peptide substrates | inhibit ATP hydrolysis, protein substrates promote ATP hydrolysis | Escherichia coli | |
3.4.21.53 | Succinyl-Phe-Ala-Phe-methoxynaphthylamide | ATP hydrolysis | Escherichia coli | |
3.4.21.53 | vanadate | ATPase inhibitor; does not inhibit but even stimulates peptide hydrolysis; inhibits protein hydrolysis | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.4.21.53 | 0.15 | - |
diphosphate | (+ peptide) | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.53 | diphosphate | activation | Escherichia coli | |
3.4.21.53 | diphosphate | in the presence of Mg2+, only peptide hydrolysis, not casein or serum albumin hydrolysis | Escherichia coli | |
3.4.21.53 | Mg2+ | requirement | Escherichia coli | |
3.4.21.53 | Mg2+ | as Mg2+-ATP | Escherichia coli | |
3.4.21.53 | Tetraphosphate | activation, only peptide hydrolysis, in the presence of Mg2+ | Escherichia coli | |
3.4.21.53 | Triphosphate | activation | Escherichia coli | |
3.4.21.53 | Triphosphate | linear triphosphate and metaphosphate | Escherichia coli | |
3.4.21.53 | Triphosphate | in the presence of Mg2+ | Escherichia coli | |
3.4.21.53 | Triphosphate | only peptide hydrolysis, not casein or serum albumin hydrolysis | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.4.21.53 | 94000 | - |
x * 94000, SDS-PAGE | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.53 | Escherichia coli | - |
K-12 | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.53 | casein + H2O | methylcasein | Escherichia coli | hydrolyzed casein | - |
? | |
3.4.21.53 | casein + H2O | methylated alpha-casein | Escherichia coli | hydrolyzed casein | - |
? | |
3.4.21.53 | CNBr-fragments of bovine serum albumin + H2O | less dependent on ATP hydrolysis | Escherichia coli | ? | - |
? | |
3.4.21.53 | Denatured bovine serum albumin + H2O | - |
Escherichia coli | ? | - |
? | |
3.4.21.53 | Globin + H2O | - |
Escherichia coli | ? | - |
? | |
3.4.21.53 | Glucagon + H2O | - |
Escherichia coli | Hydrolyzed glucagon | - |
? | |
3.4.21.53 | Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O | - |
Escherichia coli | Glutaryl-Ala-Ala-Phe + methoxynaphthylamine | - |
? | |
3.4.21.53 | additional information | no phosphorylation of enzyme or substrate during ATP hydrolysis | Escherichia coli | ? | - |
? | |
3.4.21.53 | Pancreatic polypeptide + H2O | - |
Escherichia coli | ? | - |
? | |
3.4.21.53 | Parathyroid hormone + H2O | - |
Escherichia coli | ? | - |
? | |
3.4.21.53 | Pro-His-Pro-Phe-His-Leu-Leu-Val-Tyr + H2O | nonapeptide related to equine angiotensinogen | Escherichia coli | ? | - |
? | |
3.4.21.53 | Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O | - |
Escherichia coli | Succinyl-Phe-Ala-Phe + methoxynaphthylamine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.21.53 | multimer | x * 94000, SDS-PAGE | Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.21.53 | 37 | - |
assay at | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.53 | ATP | binds to enzyme as allosteric activator allowing peptide bond hydrolysis with subsequent ATP hydrolysis | Escherichia coli | |
3.4.21.53 | ATP | activation only in the presence of Mg2+ | Escherichia coli | |
3.4.21.53 | ATP | MgATP2- rather than ATP4- | Escherichia coli | |
3.4.21.53 | ATP | splitting of high-energy bond of ATP is required for protein breakdown | Escherichia coli | |
3.4.21.53 | ATP | ATP-dependent protease | Escherichia coli | |
3.4.21.53 | ATP | ATP hydrolysis is essential for hydrolysis of proteins | Escherichia coli | |
3.4.21.53 | ATP | ATP hydrolysis is not essential for hydrolysis of peptides | Escherichia coli | |
3.4.21.53 | CTP | activation | Escherichia coli | |
3.4.21.53 | CTP | less efficient than ATP | Escherichia coli | |
3.4.21.53 | dATP | activation | Escherichia coli | |
3.4.21.53 | dATP | can replace ATP | Escherichia coli | |
3.4.21.53 | UTP | activation | Escherichia coli | |
3.4.21.53 | UTP | less efficient than ATP | Escherichia coli |