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Literature summary extracted from
- Functional and structural insights into astacin metallopeptidases (2012), Biol. Chem., 393, 1027-1041.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.21 | additional information | astacins undergo major rearrangement upon activation within an activation domain, and show a slight hinge movement when binding substrates or inhibitors. Activation of pro-astacin entails removal of the inhibiting pro-segment through successive cleavage events, which eventually replace the zinc-binding aspartate with the catalytic solvent molecule following an aspartate-switch mechanism and render the mature N-terminus at A1, enzyme activation mechanism, detailed overview | Caenorhabditis elegans | |
| 3.4.24.21 | additional information | astacins undergo major rearrangement upon activation within an activation domain, and show a slight hinge movement when binding substrates or inhibitors. Activation of pro-astacin entails removal of the inhibiting pro-segment through successive cleavage events, which eventually replace the zinc-binding aspartate with the catalytic solvent molecule following an aspartate-switch mechanism and render the mature N-terminus at A1, enzyme activation mechanism, detailed overview | Onchocerca volvulus | |
| 3.4.24.21 | additional information | astacins undergo major rearrangement upon activation within an activation domain, and show a slight hinge movement when binding substrates or inhibitors. Activation of pro-astacin entails removal of the inhibiting pro-segment through successive cleavage events, which eventually replace the zinc-binding aspartate with the catalytic solvent molecule following an aspartate-switch mechanism and render the mature N-terminus at A1, enzyme activation mechanism, detailed overview | Cyprinus carpio | |
| 3.4.24.21 | additional information | astacins undergo major rearrangement upon activation within an activation domain, and show a slight hinge movement when binding substrates or inhibitors. Activation of pro-astacin entails removal of the inhibiting pro-segment through successive cleavage events, which eventually replace the zinc-binding aspartate with the catalytic solvent molecule following an aspartate-switch mechanism and render the mature N-terminus at A1, enzyme activation mechanism, detailed overview | Trichinella spiralis | |
| 3.4.24.21 | additional information | astacins undergo major rearrangement upon activation within an activation domain, and show a slight hinge movement when binding substrates or inhibitors. Activation of pro-astacin entails removal of the inhibiting pro-segment through successive cleavage events, which eventually replace the zinc-binding aspartate with the catalytic solvent molecule following an aspartate-switch mechanism and render the mature N-terminus at A1, enzyme activation mechanism, detailed overview | Astacus astacus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.24.21 | crystal structure analysis, PDB ID 3LQ0 | Astacus astacus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.21 | cystatin C | - |
Astacus astacus | |
| 3.4.24.21 | fetiun-like protein | the enzyme circulates in the blood stream in complex with a specific protein inhibitor, formerly termed nephrosin inhibitor, which is a homologue of fetuin, a large plasma protein with many functions. Fish fetuin, like its mammalian counterpart fetuin A, contains cystatin-like domains and is related to cystatin C-like inhibitors of cysteine cathepsins | Cyprinus carpio | |
| 3.4.24.21 | fetuin-A | - |
Astacus astacus | |
| 3.4.24.21 | additional information | astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs) | Astacus astacus | |
| 3.4.24.21 | additional information | astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs) | Caenorhabditis elegans | |
| 3.4.24.21 | additional information | astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs) | Cyprinus carpio | |
| 3.4.24.21 | additional information | astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs) | Onchocerca volvulus | |
| 3.4.24.21 | additional information | astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs) | Trichinella spiralis |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.24.21 | extracellular | - |
Caenorhabditis elegans | - |
- |
| 3.4.24.21 | extracellular | - |
Onchocerca volvulus | - |
- |
| 3.4.24.21 | extracellular | - |
Cyprinus carpio | - |
- |
| 3.4.24.21 | extracellular | - |
Trichinella spiralis | - |
- |
| 3.4.24.21 | extracellular | - |
Astacus astacus | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.21 | additional information | in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion | Caenorhabditis elegans | |
| 3.4.24.21 | additional information | in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion | Onchocerca volvulus | |
| 3.4.24.21 | additional information | in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion | Cyprinus carpio | |
| 3.4.24.21 | additional information | in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion | Trichinella spiralis | |
| 3.4.24.21 | additional information | in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion | Astacus astacus | |
| 3.4.24.21 | Zn2+ | zinc metallopeptidase, the enzyme has a zinc-dependent catalytic domain with an extended zinc-binding motif, HEXXHXXGXXH, as well as three large alpha-helices and a five-stranded beta-sheet, as well as two or three disulfide bonds. The zinc-dependent moieties are divided into an N-terminal and a C-terminal sub-domain by an active-site cleft. The catalytic zinc ion resides at the bottom of the active-site cleft | Caenorhabditis elegans |  |
| 3.4.24.21 | Zn2+ | zinc metallopeptidase, the enzyme has a zinc-dependent catalytic domain with an extended zinc-binding motif, HEXXHXXGXXH, as well as three large alpha-helices and a five-stranded beta-sheet, as well as two or three disulfide bonds. The zinc-dependent moieties are divided into an N-terminal and a C-terminal sub-domain by an active-site cleft. The catalytic zinc ion resides at the bottom of the active-site cleft | Onchocerca volvulus | |
| 3.4.24.21 | Zn2+ | zinc metallopeptidase, the enzyme has a zinc-dependent catalytic domain with an extended zinc-binding motif, HEXXHXXGXXH, as well as three large alpha-helices and a five-stranded beta-sheet, as well as two or three disulfide bonds. The zinc-dependent moieties are divided into an N-terminal and a C-terminal sub-domain by an active-site cleft. The catalytic zinc ion resides at the bottom of the active-site cleft | Cyprinus carpio | |
| 3.4.24.21 | Zn2+ | zinc metallopeptidase, the enzyme has a zinc-dependent catalytic domain with an extended zinc-binding motif, HEXXHXXGXXH, as well as three large alpha-helices and a five-stranded beta-sheet, as well as two or three disulfide bonds. The zinc-dependent moieties are divided into an N-terminal and a C-terminal sub-domain by an active-site cleft. The catalytic zinc ion resides at the bottom of the active-site cleft | Trichinella spiralis | |
| 3.4.24.21 | Zn2+ | zinc metallopeptidase, the enzyme has a zinc-dependent catalytic domain with an extended zinc-binding motif, HEXXHXXGXXH, as well as three large alpha-helices and a five-stranded beta-sheet, as well as two or three disulfide bonds. The zinc-dependent moieties are divided into an N-terminal and a C-terminal sub-domain by an active-site cleft. The catalytic zinc ion resides at the bottom of the active-site cleft | Astacus astacus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.21 | Astacus astacus | P07584 | - |
- |
| 3.4.24.21 | Caenorhabditis elegans | - |
diverse genes | - |
| 3.4.24.21 | Cyprinus carpio | - |
- |
- |
| 3.4.24.21 | Onchocerca volvulus | - |
- |
- |
| 3.4.24.21 | Trichinella spiralis | - |
diverse genes | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.24.21 | proteolytic modification | the enzyme is synthesized as inactive zymogen, the N-terminal pro-segments are variable in length and rather unstructured, astacin-family zymogen structure, overview. They inhibit the catalytic zinc following an aspartate-switch mechanism mediated by an aspartate embedded in a conserved motif, FXGD. Removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1' | Caenorhabditis elegans |
| 3.4.24.21 | proteolytic modification | the enzyme is synthesized as inactive zymogen, the N-terminal pro-segments are variable in length and rather unstructured, astacin-family zymogen structure, overview. They inhibit the catalytic zinc following an aspartate-switch mechanism mediated by an aspartate embedded in a conserved motif, FXGD. Removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1' | Onchocerca volvulus |
| 3.4.24.21 | proteolytic modification | the enzyme is synthesized as inactive zymogen, the N-terminal pro-segments are variable in length and rather unstructured, astacin-family zymogen structure, overview. They inhibit the catalytic zinc following an aspartate-switch mechanism mediated by an aspartate embedded in a conserved motif, FXGD. Removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1' | Cyprinus carpio |
| 3.4.24.21 | proteolytic modification | the enzyme is synthesized as inactive zymogen, the N-terminal pro-segments are variable in length and rather unstructured, astacin-family zymogen structure, overview. They inhibit the catalytic zinc following an aspartate-switch mechanism mediated by an aspartate embedded in a conserved motif, FXGD. Removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1' | Trichinella spiralis |
| 3.4.24.21 | proteolytic modification | the enzyme is synthesized as inactive zymogen, the N-terminal pro-segments are variable in length and rather unstructured, astacin-family zymogen structure, overview. They inhibit the catalytic zinc following an aspartate-switch mechanism mediated by an aspartate embedded in a conserved motif, FXGD. Removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1' | Astacus astacus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.24.21 | blood | - |
Cyprinus carpio | - |
| 3.4.24.21 | head kidney | - |
Cyprinus carpio | - |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.24.21 | More | astacins structure comparisons, detailed overview | Caenorhabditis elegans |
| 3.4.24.21 | More | astacins structure comparisons, detailed overview | Onchocerca volvulus |
| 3.4.24.21 | More | astacins structure comparisons, detailed overview | Cyprinus carpio |
| 3.4.24.21 | More | astacins structure comparisons, detailed overview | Trichinella spiralis |
| 3.4.24.21 | More | astacins structure comparisons, detailed overview | Astacus astacus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.24.21 | astacin metallopeptidases | - |
Caenorhabditis elegans |
| 3.4.24.21 | astacin metallopeptidases | - |
Onchocerca volvulus |
| 3.4.24.21 | astacin metallopeptidases | - |
Cyprinus carpio |
| 3.4.24.21 | astacin metallopeptidases | - |
Trichinella spiralis |
| 3.4.24.21 | astacin metallopeptidases | - |
Astacus astacus |
| 3.4.24.21 | Astacus protease | - |
Astacus astacus |
| 3.4.24.21 | crayfish small-molecule protease | - |
Astacus astacus |
| 3.4.24.21 | More | formerly termed nephrosin | Cyprinus carpio |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.24.21 | evolution | the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview | Caenorhabditis elegans |
| 3.4.24.21 | evolution | the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview | Onchocerca volvulus |
| 3.4.24.21 | evolution | the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview | Cyprinus carpio |
| 3.4.24.21 | evolution | the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview | Trichinella spiralis |
| 3.4.24.21 | evolution | the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview | Astacus astacus |
| 3.4.24.21 | additional information | removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket S1' | Trichinella spiralis |
| 3.4.24.21 | additional information | removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1' | Caenorhabditis elegans |
| 3.4.24.21 | additional information | removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1' | Onchocerca volvulus |
| 3.4.24.21 | additional information | removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1' | Cyprinus carpio |
| 3.4.24.21 | additional information | removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1' | Astacus astacus |
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