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Information on EC 3.4.24.21 - astacin and Organism(s) Caenorhabditis elegans and UniProt Accession P98060

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.21 astacin
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This record set is specific for:
Caenorhabditis elegans
UNIPROT: P98060 not found.
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'
Synonyms
astacin, ovastacin, toxin 3, mep1b, dpy-31, nephrosin, astacin metalloprotease, astacin-like metalloprotease, nas-37, astacus protease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
astacin metalloprotease
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Procollagen C-proteinase
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astacin metallopeptidases
-
-
Astacus proteinase
-
-
-
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Crayfish small-molecule proteinase
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-
-
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nas-36
nas-37
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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hydrolysis of arylamide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
143179-21-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
a zinc metalloprotease
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
additional information
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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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-[3-(1-aminoethenyl)-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
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6-cyclohexyl-3-[3-(2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
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6-cyclohexyl-3-[3-[4-(dihydroxymethyl)pyridin-2-yl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
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6-cyclohexyl-N-hydroxy-3-(3-[1-[(methylsulfonyl)amino]ethenyl]-1,2,4-oxadiazol-5-yl)hexanamide
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additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene dpy-31
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme inhibition causes body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis. Enzyme mutation causes temperature-sensitive lethality and cuticle defects, a DPY-31 enzyme from the ovine gastrointestinal nematode Teladorsagia circumcincta mutant strain TP224 is able to rescue the Caenorhabditis elegans mutant
physiological function
the enzyme is a homologue of a vertebrate procollagen C-proteinase and performs a central role in cuticle formation of Caenorhabditis elegans
evolution
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the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview
malfunction
additional information
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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'
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NAS35_CAEEL
592
0
67257
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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astacins structure comparisons, detailed overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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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'
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dpy-31, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stepek, G.; McCormack, G.; Page, A.
Collagen processing and cuticle formation is catalysed by the astacin metalloprotease DPY-31 in free-living and parasitic nematodes
Int. J. Parasitol.
40
533-542
2010
Brugia malayi, Caenorhabditis elegans, Haemonchus contortus
Manually annotated by BRENDA team
Stepek, G.; McCormack, G.; Birnie, A.J.; Page, A.P.
The astacin metalloprotease moulting enzyme NAS-36 is required for normal cuticle ecdysis in free-living and parasitic nematodes
Parasitology
138
237-248
2011
Brugia malayi, Caenorhabditis elegans
Manually annotated by BRENDA team
Gomis-Rueth, F.X.; Trillo-Muyo, S.; Stoecker, W.
Functional and structural insights into astacin metallopeptidases
Biol. Chem.
393
1027-1041
2012
Caenorhabditis elegans, Cyprinus carpio, Onchocerca volvulus, Trichinella spiralis, Astacus astacus (P07584)
Manually annotated by BRENDA team
Stepek, G.; McCormack, G.; Winter, A.D.; Page, A.P.
A highly conserved, inhibitable astacin metalloprotease from Teladorsagia circumcincta is required for cuticle formation and nematode development
Int. J. Parasitol.
45
345-355
2015
Caenorhabditis elegans (P98060), Caenorhabditis elegans, Caenorhabditis elegans N2 (P98060), Haemonchus contortus (D5FM33), Haemonchus contortus, Haemonchus contortus ISE (D5FM33), Teladorsagia circumcincta (A0A0C5PRQ1), Teladorsagia circumcincta, Teladorsagia circumcincta MTci5 (A0A0C5PRQ1)
Manually annotated by BRENDA team