EC Number   |
General Information |
Reference |
|---|
   3.4.24.63 | evolution |
human meprin beta ia a single-zinc metalloendoprotease of the astacin family |
755294 |
| 3.4.24.63 | evolution |
meprin beta belongs to the astacin family of zinc-endopeptidases and the metzincin superfamily, characterized by the conserved motif HExxHxxGxxHxxxRxDR. Meprin beta is the only membrane-bound member of the astacin family |
754592 |
| 3.4.24.63 | evolution |
meprin beta belongs to the astacin family within the metzincins, with a tight 1,4-beta-type Met turn located below the catalytic zinc site, featuring a strictly conserved methionine, M209 |
735161 |
| 3.4.24.63 | evolution |
meprin beta belongs to the astacins of the metzincin superfamily |
-, 753536 |
| 3.4.24.63 | evolution |
meprin beta is a metalloprotease of the astacin family characterized by a conserved zinc-binding motif (HExxHxxGFxHExxRxDR). Human meprin-alpha, EC 3.4.24.18, and -beta protease subunits are 55% identical at the amino acid level, while the substrate and peptide bond specificities vary markedly |
734332 |
| 3.4.24.63 | evolution |
meprin metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily |
733288 |
| 3.4.24.63 | evolution |
meprin metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily. Meprins belong to the astacin family of metalloproteases, comprising only six members in humans. These enzymes are characterized by a conserved zinc-binding motif (HExxHxxGxxHxxxRxDR) and by a sequence in close proximity to the active-site cleft, the so called Met-turn, that includes a tyrosine residue as a fifth zinc ligand. Within the astacin family, meprins exhibit a unique domain composition |
733288 |
| 3.4.24.63 | evolution |
the astacin proteases meprin alpha and meprin beta are zinc-dependent metalloproteases of the metzincin superfamily |
752474 |
| 3.4.24.63 | evolution |
the enzyme belongs to the astacin protease family |
734193 |
| 3.4.24.63 | evolution |
the enzyme encoded by Mmepb belongs to the BTP 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 and docking study, and potential binding site, detailed overview |
753345 |
