Matches in DBpedia 2016-04 for { ?s ?p "Candoxatril is the orally active prodrug of candoxatrilat (UK-73967) human neutral endopeptidase (Neprilysin) as the neutral endopeptidase 24.11 complexed (RB-101) with phosphoramidon degrades and inactivates a number of bioactive peptides. Two multiply connected folding domains of the neutral endopeptidase locus splicing of exons 1, 2a, or 2b to the common exon 3 composed of 24 exons of the human CALLA/NEP gene containing the active site, it is known as peptidase family M13 (neprilysin family, clan MA(E)) the gluzincins a faint but significant structural relationship of the metzincins to the thermolysin-like enzymes, Zincin is the simplest descriptor of biological space. The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site of the 5-indanyl ester prodrug candoxatril and differs from phosphoramidon [N-(N-(((6-Deoxy-α-L-mannopyranosyl)oxy)hydroxyphosphinyl)-L- leucyl)-L-tryptophan] in several respects the structure of human neutral endopeptidase complexed with phosphoramidon is lost due to desolvation of the enzyme and ligand on formation of the complex Candoxatril."@en }
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- Candoxatril abstract "Candoxatril is the orally active prodrug of candoxatrilat (UK-73967) human neutral endopeptidase (Neprilysin) as the neutral endopeptidase 24.11 complexed (RB-101) with phosphoramidon degrades and inactivates a number of bioactive peptides. Two multiply connected folding domains of the neutral endopeptidase locus splicing of exons 1, 2a, or 2b to the common exon 3 composed of 24 exons of the human CALLA/NEP gene containing the active site, it is known as peptidase family M13 (neprilysin family, clan MA(E)) the gluzincins a faint but significant structural relationship of the metzincins to the thermolysin-like enzymes, Zincin is the simplest descriptor of biological space. The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site of the 5-indanyl ester prodrug candoxatril and differs from phosphoramidon [N-(N-(((6-Deoxy-α-L-mannopyranosyl)oxy)hydroxyphosphinyl)-L- leucyl)-L-tryptophan] in several respects the structure of human neutral endopeptidase complexed with phosphoramidon is lost due to desolvation of the enzyme and ligand on formation of the complex Candoxatril.".
- Q5032033 abstract "Candoxatril is the orally active prodrug of candoxatrilat (UK-73967) human neutral endopeptidase (Neprilysin) as the neutral endopeptidase 24.11 complexed (RB-101) with phosphoramidon degrades and inactivates a number of bioactive peptides. Two multiply connected folding domains of the neutral endopeptidase locus splicing of exons 1, 2a, or 2b to the common exon 3 composed of 24 exons of the human CALLA/NEP gene containing the active site, it is known as peptidase family M13 (neprilysin family, clan MA(E)) the gluzincins a faint but significant structural relationship of the metzincins to the thermolysin-like enzymes, Zincin is the simplest descriptor of biological space. The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site of the 5-indanyl ester prodrug candoxatril and differs from phosphoramidon [N-(N-(((6-Deoxy-α-L-mannopyranosyl)oxy)hydroxyphosphinyl)-L- leucyl)-L-tryptophan] in several respects the structure of human neutral endopeptidase complexed with phosphoramidon is lost due to desolvation of the enzyme and ligand on formation of the complex Candoxatril.".