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Literature summary extracted from
- Structure-activity relationship of astacin metalloproteases A comparative study using EDTA (2018), Curr. Enzyme Inhib., 14, 131-140 .
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.24.18 | gene Mep1A, sequence comparisons | Mus musculus |
| 3.4.24.18 | gene Mep1A, sequence comparisons | Rattus norvegicus |
| 3.4.24.19 | gene dtld, sequence comparisons | Drosophila melanogaster |
| 3.4.24.19 | gene mbmp1, sequence comparisons | Mus musculus |
| 3.4.24.19 | gene Xebmp1, sequence comparisons | Xenopus laevis |
| 3.4.24.21 | gene ASTL, sequence comparisons | Homo sapiens |
| 3.4.24.21 | gene qcam1, sequence comparisons | Coturnix japonica |
| 3.4.24.63 | gene Mep1B, sequence comparisons | Mus musculus |
| 3.4.24.63 | gene Mep1B, sequence comparisons | Rattus norvegicus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.18 | EDTA | a common inhibitor of several astacin metalloproteases | Mus musculus |  |
| 3.4.24.18 | EDTA | a common inhibitor of several astacin metalloproteases | Rattus norvegicus | |
| 3.4.24.19 | EDTA | a common inhibitor of several astacin metalloproteases | Drosophila melanogaster | |
| 3.4.24.19 | EDTA | a common inhibitor of several astacin metalloproteases | Mus musculus | |
| 3.4.24.19 | EDTA | a common inhibitor of several astacin metalloproteases | Xenopus laevis | |
| 3.4.24.21 | EDTA | a common inhibitor of several astacin metalloproteases | Coturnix japonica | |
| 3.4.24.21 | EDTA | a common inhibitor of several astacin metalloproteases | Homo sapiens | |
| 3.4.24.63 | EDTA | a common inhibitor of several astacin metalloproteases | Mus musculus | |
| 3.4.24.63 | EDTA | a common inhibitor of several astacin metalloproteases | Rattus norvegicus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.24.18 | extracellular | - |
Mus musculus | - |
- |
| 3.4.24.18 | extracellular | - |
Rattus norvegicus | - |
- |
| 3.4.24.19 | extracellular | - |
Mus musculus | - |
- |
| 3.4.24.19 | extracellular | - |
Xenopus laevis | - |
- |
| 3.4.24.19 | extracellular | - |
Drosophila melanogaster | - |
- |
| 3.4.24.21 | extracellular | - |
Coturnix japonica | - |
- |
| 3.4.24.21 | extracellular | - |
Homo sapiens | - |
- |
| 3.4.24.63 | membrane | membrane-bound | Mus musculus | 16020 | - |
| 3.4.24.63 | membrane | membrane-bound | Rattus norvegicus | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.18 | Zn2+ | zinc metalloproteinase | Mus musculus | |
| 3.4.24.18 | Zn2+ | zinc metalloproteinase | Rattus norvegicus | |
| 3.4.24.19 | Zn2+ | zinc metalloproteinase | Mus musculus | |
| 3.4.24.19 | Zn2+ | zinc metalloproteinase | Xenopus laevis | |
| 3.4.24.19 | Zn2+ | zinc metalloproteinase | Drosophila melanogaster | |
| 3.4.24.21 | Zn2+ | zinc metalloproteinase | Coturnix japonica | |
| 3.4.24.21 | Zn2+ | zinc metalloproteinase | Homo sapiens | |
| 3.4.24.63 | Zn2+ | zinc metalloproteinase | Mus musculus | |
| 3.4.24.63 | Zn2+ | zinc metalloproteinase | Rattus norvegicus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.18 | Mus musculus | P28825 | - |
- |
| 3.4.24.18 | Rattus norvegicus | Q64230 | - |
- |
| 3.4.24.19 | Drosophila melanogaster | P25723 | - |
- |
| 3.4.24.19 | Mus musculus | P98063 | - |
- |
| 3.4.24.19 | Xenopus laevis | P98070 | - |
- |
| 3.4.24.21 | Coturnix japonica | P42662 | - |
- |
| 3.4.24.21 | Homo sapiens | Q6HA08 | - |
- |
| 3.4.24.63 | Mus musculus | Q61847 | - |
- |
| 3.4.24.63 | Rattus norvegicus | P28826 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.24.18 | MEP1A | - |
Mus musculus |
| 3.4.24.18 | MEP1A | - |
Rattus norvegicus |
| 3.4.24.18 | meprin alpha | - |
Mus musculus |
| 3.4.24.18 | meprin alpha | - |
Rattus norvegicus |
| 3.4.24.18 | Mmepa | - |
Mus musculus |
| 3.4.24.18 | Rmepa | - |
Rattus norvegicus |
| 3.4.24.19 | BMP-1 | - |
Mus musculus |
| 3.4.24.19 | BMP-1 | - |
Xenopus laevis |
| 3.4.24.19 | bone morphogenetic protein 1 | - |
Mus musculus |
| 3.4.24.19 | bone morphogenetic protein 1 | - |
Xenopus laevis |
| 3.4.24.19 | dorsal-ventral patterning protein tolloid | - |
Drosophila melanogaster |
| 3.4.24.19 | Tld | - |
Drosophila melanogaster |
| 3.4.24.21 | astacin-like metalloendopeptidase | UniProt | Coturnix japonica |
| 3.4.24.21 | astacin-like metalloendopeptidase | UniProt | Homo sapiens |
| 3.4.24.21 | ASTL | - |
Homo sapiens |
| 3.4.24.21 | Ovastacin | - |
Homo sapiens |
| 3.4.24.21 | Qcam1 | - |
Coturnix japonica |
| 3.4.24.63 | MEP1B | - |
Mus musculus |
| 3.4.24.63 | MEP1B | - |
Rattus norvegicus |
| 3.4.24.63 | meprin beta | - |
Mus musculus |
| 3.4.24.63 | meprin beta | - |
Rattus norvegicus |
| 3.4.24.63 | Mmepb | - |
Mus musculus |
| 3.4.24.63 | Rmepb | - |
Rattus norvegicus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.24.18 | 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 |
| 3.4.24.18 | 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 |
| 3.4.24.18 | 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 |
| 3.4.24.18 | 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 |
| 3.4.24.19 | evolution | the enzyme encoded by bmp1 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 (template crystal structure PDB ID 3EDH) and docking study, and potential binding site, detailed overview | Xenopus laevis |
| 3.4.24.19 | evolution | the enzyme encoded by bmp1 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 |
| 3.4.24.19 | evolution | the enzyme encoded by tld 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 | Drosophila melanogaster |
| 3.4.24.19 | additional information | the hydrogen bonding residue of the enzyme is Glu219, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3EDH) and docking study, and potential binding site, detailed overview | Mus musculus |
| 3.4.24.19 | additional information | the hydrogen bonding residues of the enzyme are Glu232, Ser294, and Tyr290, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3EDH) and docking study, and potential binding site, detailed overview | Drosophila melanogaster |
| 3.4.24.19 | additional information | the hydrogen bonding residues of the enzyme are Ser163, Tyr235, and Arg265, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview | Xenopus laevis |
| 3.4.24.21 | evolution | the enzyme encoded by ASTL belongs to the digestive and hatching enzymes 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 (template crystal structure PDB ID 3LQB) and docking study, and potential binding site, detailed overview | Homo sapiens |
| 3.4.24.21 | evolution | the enzyme encoded by qcam1 belongs to the digestive and hatching enzymes 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 (template crystal structure PDB ID 3LQB) and docking study, and potential binding site, detailed overview | Coturnix japonica |
| 3.4.24.21 | additional information | the hydrogen bonding residues of the enzyme are Ser155, His186, His192, Tyr238, and Asn217, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview | Homo sapiens |
| 3.4.24.21 | additional information | the hydrogen bonding residues of the enzyme are Tyr60, His84, Glu85, His88, His94, and Asp119, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview | Coturnix japonica |
| 3.4.24.63 | evolution | the enzyme encoded by Mmepb 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 |
| 3.4.24.63 | evolution | the enzyme encoded by Rmepb 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 |
| 3.4.24.63 | additional information | the hydrogen bonding residues of the enzyme are Cys125, Glu154, and Arg239, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview | Mus musculus |
| 3.4.24.63 | additional information | the hydrogen bonding residues of the enzyme are Cys125, Thr150, Tyr212, and His211, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview | Rattus norvegicus |
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