3.4.24.21: astacin
This is an abbreviated version!
For detailed information about astacin, go to the full flat file.
Reaction
Hydrolysis of peptide bonds in substrates containing five or additional information amino acids, preferentially with Ala in P1', and Pro in P2'
=
Synonyms
Ace-MTP-2, Ancylostoma ceylanicum metalloprotease 2, Ast1, Ast2, Ast3, Ast4, Ast5, Ast6, Ast7, Ast9, astacin, astacin metallopeptidases, astacin metalloprotease, astacin-like metalloendopeptidase, astacin-like metalloprotease, astacin-like metalloprotease toxin 3, astacin-Like protease 3, Astacus protease, Astacus proteinase, ASTL, BMP-1, bone morphogenetic protein 1, carp nephrosin, crayfish small-molecule protease, Crayfish small-molecule proteinase, DPY-31, EC 3.4.99.6, LALP3, LAST, LAST_MAM, MEP1A, MEP1B, More, NAS-35, nas-36, nas-37, nephrosin, Ovastacin, Procollagen C-proteinase, Qcam1, Sc-AST, Smed-ast-1, Smed-ast-2, Smed-ast-3, Smed-ast-4, Smed-ast-5, Smed-ast-6, Smed-ast-7, Smed-ast-9, toxin 3, Xhe2
ECTree
Posttranslational Modification
Posttranslational Modification on EC 3.4.24.21 - astacin
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phosphoprotein
the protease has a putative signal peptide, 11 potential phosphorylation sites, and two disulfide bridges revealed by computational analysis
glycoprotein
-
putative
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'
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'
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'
proteolytic modification
in active BMP-1 an additional ion seems to be coordinated by several residues. The new N-terminus that results from intracellular activation of BMP-1, Ala121, is acetylated (N-Ace A121) and, together with Glu224, Asp312 and three water molecules, it interacts with this ion, overview
proteolytic modification
-
both LAST and LAST_MAM are synthesized as zymogens. LAST-MAM is active in its zymogen form
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'
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'