EC Number   |
General Information |
Reference |
|---|
   3.4.24.18 | evolution |
meprin A, is a membrane-associated neutral metalloendoprotease that belongs to the astacin family of zinc endopeptidases |
-, 733064 |
| 3.4.24.18 | evolution |
meprin alpha belongs to the astacin family of zinc-endopeptidases and the metzincin superfamily, characterized by the conserved motif HExxHxxGxxHxxxRxDR |
754593 |
| 3.4.24.18 | evolution |
meprin alpha is a metalloprotease of the astacin family characterized by a conserved zinc-binding motif (HExxHxxGFxHExxRxDR). Human meprin-alpha and -beta protease, EC 3.4.24.63, subunits are 55% identical at the amino acid level, while the substrate and peptide bond specificities vary markedly |
734332 |
| 3.4.24.18 | evolution |
meprin metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily |
733288 |
| 3.4.24.18 | 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 |
| 3.4.24.18 | evolution |
the astacin proteases meprin alpha and meprin beta are zinc-dependent metalloproteases of the metzincin superfamily |
752474 |
| 3.4.24.18 | evolution |
the enzyme encoded by Mmepa 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 |
| 3.4.24.18 | evolution |
the enzyme encoded by Rmepa 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 |
| 3.4.24.18 | malfunction |
altered localization and shedding of meprin A in places other than the apical membranes may be deleterious in vivo in acute tubular injury. Importance of a sheddase involved in the release of membrane-associated meprin A under pathological conditions |
-, 733064 |
| 3.4.24.18 | malfunction |
breast cancer MDA-MB-435 cells treated with the meprin inhibitor actinonin are less invasive in vitro. Altered localization and shedding of meprin A in places other than the apical membranes may be deleterious in vivo in acute tubular injury. Importance of a sheddase involved in the release of membrane-associated meprin A under pathological conditions |
733064 |
