Cloned (Comment) | Organism |
---|---|
gene Mep1A, sequence comparisons | Mus musculus |
gene Mep1A, sequence comparisons | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EDTA | a common inhibitor of several astacin metalloproteases | Mus musculus | |
EDTA | a common inhibitor of several astacin metalloproteases | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Mus musculus | - |
- |
extracellular | - |
Rattus norvegicus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | zinc metalloproteinase | Mus musculus | |
Zn2+ | zinc metalloproteinase | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | P28825 | - |
- |
Rattus norvegicus | Q64230 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
MEP1A | - |
Mus musculus |
MEP1A | - |
Rattus norvegicus |
meprin alpha | - |
Mus musculus |
meprin alpha | - |
Rattus norvegicus |
Mmepa | - |
Mus musculus |
Rmepa | - |
Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme encoded by Mmepa belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview | Mus musculus |
evolution | the enzyme encoded by Rmepa belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview | Rattus norvegicus |
additional information | the hydrogen bonding residues of the enzyme are Ser131, Glu157, His166, Ser169, and Tyr195, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview | Rattus norvegicus |
additional information | the hydrogen bonding residues of the enzyme are Thr151 and Leu210, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview | Mus musculus |