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Literature summary for 3.4.24.21 extracted from

  • Gomis-Rueth, F.X.; Trillo-Muyo, S.; Stoecker, W.
    Functional and structural insights into astacin metallopeptidases (2012), Biol. Chem., 393, 1027-1041.
    View publication on PubMed

Activating Compound

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 (Commentary)

Crystallization (Comment) Organism
crystal structure analysis, PDB ID 3LQ0 Astacus astacus

Inhibitors

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

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Caenorhabditis elegans
-
-
extracellular
-
Onchocerca volvulus
-
-
extracellular
-
Cyprinus carpio
-
-
extracellular
-
Trichinella spiralis
-
-
extracellular
-
Astacus astacus
-
-

Metals/Ions

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

Organism UniProt Comment Textmining
Astacus astacus P07584
-
-
Caenorhabditis elegans
-
diverse genes
-
Cyprinus carpio
-
-
-
Onchocerca volvulus
-
-
-
Trichinella spiralis
-
diverse genes
-

Posttranslational Modification

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

Source Tissue Comment Organism Textmining
blood
-
Cyprinus carpio
-
head kidney
-
Cyprinus carpio
-

Subunits

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

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

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