Activating Compound | Comment | Organism | Structure |
---|---|---|---|
H2O2 | - |
Homo sapiens | |
H2O2 | synergistic effect of antimycin A, succinate, and antimycin A plus succinate on activation by H2O2. Antimycin A and succinate stimulate the H2O2 production and increase rTOP activity | Rattus norvegicus |
Cloned (Comment) | Organism |
---|---|
gene Thop1, recombinant expression of wild-type and mutant enzymes | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
C246S/C248S/C253S | site-directed mutagenesis, the mutations abolish the DTT and H2O2 effects on rTOP activity. The triple-mutated rTOP is not affected by DTT | Rattus norvegicus |
General Stability | Organism |
---|---|
H2O2 stabilizes the monomeric enzyme form | Rattus norvegicus |
H2O2 stabilizes the monomeric enzyme form | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
DTT | - |
Homo sapiens | |
DTT | - |
Rattus norvegicus | |
JA-2 | specific inhibition | Homo sapiens | |
JA-2 | specific inhibition | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Rattus norvegicus | 5829 | - |
cytosol | - |
Homo sapiens | 5829 | - |
mitochondrion | - |
Rattus norvegicus | 5739 | - |
mitoplast | - |
Rattus norvegicus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | a zinc metalloproteinase | Rattus norvegicus | |
Zn2+ | a zinc metalloproteinase | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P52888 | - |
- |
Rattus norvegicus | P24155 | - |
- |
Oxidation Stability | Organism |
---|---|
H2O2 activates the enzyme | Rattus norvegicus |
H2O2 activates the enzyme | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
HEK-293 cell | - |
Homo sapiens | - |
liver | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Abz-GFSPFRQ-EDDnp + H2O | - |
Rattus norvegicus | ? | - |
? | |
Abz-GFSPFRQ-EDDnp + H2O | - |
Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Rattus norvegicus |
dimer | - |
Homo sapiens |
monomer | active form, stabilized by H2O2 | Rattus norvegicus |
monomer | active form, stabilized by H2O2 | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
THOP1 | - |
Rattus norvegicus |
THOP1 | - |
Homo sapiens |
TOP | - |
Rattus norvegicus |
TOP | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | redox modulation of thimet oligopeptidase activity by hydrogen peroxide | Rattus norvegicus |
additional information | redox modulation of thimet oligopeptidase activity by hydrogen peroxide | Homo sapiens |
physiological function | thimet oligopeptidase (TOP) can process a diversity of bioactive peptides. TOP is one of the main postproteasomal enzymes that process peptide antigens in the MHC class I presentation route. Fine regulation of TOP activity by hydrogen peroxide | Homo sapiens |
physiological function | thimet oligopeptidase (TOP) can process a diversity of bioactive peptides. TOP is one of the main postproteasomal enzymes that process peptide antigens in the MHC class I presentation route. Fine regulation of TOP activity by hydrogen peroxide. Contrary to the oxidation produced by aging associated with enzyme oligomerization and inhibition, H2O2 oxidation produces sulfenic acid and maintains recombinant TOP in the monomeric form. Consistent with the involvement of rTOP in a signaling redox cascade, the H2O2-oxidized recombinant TOP reacts with dimeric thioredoxin-1 (TRx-1) and remains covalently bound to one subunit of TRx-1 | Rattus norvegicus |