Activating Compound | Comment | Organism | Structure |
---|---|---|---|
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 | |
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 | |
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 | |
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 | |
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 (Comment) | Organism |
---|---|
crystal structure analysis, PDB ID 3LQ0 | Astacus astacus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
cystatin C | - |
Astacus astacus | |
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 | |
fetuin-A | - |
Astacus astacus | |
additional information | astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs) | Astacus astacus | |
additional information | astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs) | Caenorhabditis elegans | |
additional information | astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs) | Cyprinus carpio | |
additional information | astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs) | Onchocerca volvulus | |
additional information | astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs) | Trichinella spiralis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Caenorhabditis elegans | - |
- |
extracellular | - |
Onchocerca volvulus | - |
- |
extracellular | - |
Cyprinus carpio | - |
- |
extracellular | - |
Trichinella spiralis | - |
- |
extracellular | - |
Astacus astacus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Astacus astacus | P07584 | - |
- |
Caenorhabditis elegans | - |
diverse genes | - |
Cyprinus carpio | - |
- |
- |
Onchocerca volvulus | - |
- |
- |
Trichinella spiralis | - |
diverse genes | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
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 |
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 |
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 |
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 |
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 | Comment | Organism | Textmining |
---|---|---|---|
blood | - |
Cyprinus carpio | - |
head kidney | - |
Cyprinus carpio | - |
Subunits | Comment | Organism |
---|---|---|
More | astacins structure comparisons, detailed overview | Caenorhabditis elegans |
More | astacins structure comparisons, detailed overview | Onchocerca volvulus |
More | astacins structure comparisons, detailed overview | Cyprinus carpio |
More | astacins structure comparisons, detailed overview | Trichinella spiralis |
More | astacins structure comparisons, detailed overview | Astacus astacus |
Synonyms | Comment | Organism |
---|---|---|
astacin metallopeptidases | - |
Caenorhabditis elegans |
astacin metallopeptidases | - |
Onchocerca volvulus |
astacin metallopeptidases | - |
Cyprinus carpio |
astacin metallopeptidases | - |
Trichinella spiralis |
astacin metallopeptidases | - |
Astacus astacus |
Astacus protease | - |
Astacus astacus |
crayfish small-molecule protease | - |
Astacus astacus |
More | formerly termed nephrosin | Cyprinus carpio |
General Information | Comment | Organism |
---|---|---|
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |