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Literature summary for 3.4.24.18 extracted from

  • Chaudhuri, A.; Sarkar, I.; Chakraborty, S.
    Comparative analysis of binding sites of human meprins with hydroxamic acid derivative by molecular dynamics simulation study (2014), J. Biomol. Struct. Dyn., 32, 1969-1978.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information binding sites and binding structure of hydroxamic acid derivative inhibitors, molecular dynamics simulation study, overview Homo sapiens
Pro-Leu-Gly-hydroxamate binding structure in S subsites, overview. A decrease in solvent accessibility values at specific residues upon inhibitor binding occurs. The S subsite of the enzyme interacts with residues at P site of the inhibitor Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ meprin alpha is a metalloprotease of the astacin family characterized by a conserved zinc-binding motif (HExxHxxGFxHExxRxDR) Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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General Information

General Information Comment Organism
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 Homo sapiens
additional information homology modeling of the protease domain of meprin alpha on the astacin crystal structure and molecular dynamics simulation study, overview Homo sapiens