EC Number   |
General Information |
Reference |
|---|
   3.4.24.21 | evolution |
structural organization of the astacin-like gene family in planarians, overview. All members of the astacin family are characterized by two key elements: the 18-amino acid zinc-binding motif (HEXXHXXGFXHEXXRXDR), and the methionine-turn (Met-turn) sequence SXMHY |
753733 |
| 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 |
733445 |
| 3.4.24.21 | evolution |
the enzyme belongs to the astacin family of zinc-dependent endopeptidase. All the members of this family have a protease domain containing approximately 200 amino acids, which shares an amino-acid sequence similarity of 29-99%. Astacin family members are characterized by a unique 18 amino acid signature sequence HEXXHXXGFXHEXXRXDR containing the Zn binding motif HEXXH present in all metalloendopeptidases. Most of the known family members contain a COOH terminal to the protease domain. They are found to contain one or more copies of the EGF (epidermal growth factor) like E and/or CUB (complement subcomponents) domain. Differences in the active sites and inhibitor sites of astacin/BMP1, human meprin alpha, and human meprin beta, overview. The subsites S1, S2, S3, S1', S2', S3' have differences in amino acid residues. Structure homology modelling |
753328 |
| 3.4.24.21 | evolution |
the enzyme belongs to the family of extracellular zinc peptidases, termed stacin family, and of the metzincin superfamily |
734420 |
| 3.4.24.21 | evolution |
the enzyme encoded by ASTL belongs to the digestive and hatching enzymes cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3LQB) and docking study, and potential binding site, detailed overview |
753345 |
| 3.4.24.21 | evolution |
the enzyme encoded by qcam1 belongs to the digestive and hatching enzymes cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3LQB) and docking study, and potential binding site, detailed overview |
753345 |
| 3.4.24.21 | evolution |
the enzyme is a member of the astacin family of metalloproteases |
733941 |
| 3.4.24.21 | malfunction |
ablation of one of the two zinc metalloproteinases, meprin beta and BMP-1, leads to different collagen I associated phenotypes in vivo |
753172 |
| 3.4.24.21 | malfunction |
enzyme inhibition causes body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis |
-, 734008 |
| 3.4.24.21 | 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 |
-, 734008 |
