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Literature summary extracted from

  • Machado, M.F.; Cunha, F.M.; Berti, D.A.; Heimann, A.S.; Klitzke, C.F.; Rioli, V.; Oliveira, V.; Ferro, E.S.
    Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme (2006), Biochem. Biophys. Res. Commun., 339, 520-525.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.15 L-phospho-Thr-Leu-Arg-Thr-Lys-Leu comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme Sus scrofa
3.4.24.15 LTLRTKL comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme Sus scrofa
3.4.24.15 LVVYPW-phenylThr-Gln-Arg-Tyr comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme Sus scrofa
3.4.24.15 LVVYPWTQRY comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme Sus scrofa
3.4.24.15 additional information phosphorylation of substrates reduces catalytic activity, phosphorylation of competitive inhibitors only alters their Ki-values Sus scrofa
3.4.24.15 VVYPW-phenylThr-Gln-Arg-Tyr comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme Sus scrofa
3.4.24.15 VVYPWTQRY comparison with inhibitory effect on EC3.4.24.16 and angiotensin-converting enzyme Sus scrofa
3.4.24.16 additional information putative intracellular peptides as competetive inhibitors of (o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) hydrolysis by EP24.16 More

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.15 Sus scrofa
-
-
-
3.4.24.16 More
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.15 2-aminobenzoyl-GFSHFRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
-
 Sus scrofa 2-aminobenzoyl-GFSH + FRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
 ?
3.4.24.15 LTLRTKL + H2O at 91% of the rate with RPPGF-SP-FR Sus scrofa LTLR + Thr + Lys-Leu
-
 ?
3.4.24.15 additional information phosphorylation of substrates reduces catalytic activity, phosphorylation of competitive inhibitors only alters their Ki-values Sus scrofa ?
-
 ?
3.4.24.15 pTLRTKL + H2O at 10% of the rate with RPPGF-SP-FR Sus scrofa phospho-Thr-Leu-Arg + L-tyrosine + Lys-Leu
-
 ?
3.4.24.15 RPPGFSPFR + H2O
-
 Sus scrofa RPPGF + Ser-Pro + Phe-Arg
-
 ?
3.4.24.15 VVYPW-TQ-RY-KL + H2O at 9% of the rate with RPPGF-SP-FR Sus scrofa VVYPW + Thr-Gln + Arg-Tyr + Lys-Leu
-
 ?
3.4.24.16 (o-aminobenzoyl)-GFSHFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
-
 More (o-aminobenzoyl)-GFSH + FRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
 ?
3.4.24.16 bradykinin + H2O
-
 More ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.16 ep24.16
-
 More

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.24.15 0.0008
-
 LVVYPW-phenylThr-Gln-Arg-Tyr pH 8.0, 37°C Sus scrofa
3.4.24.15 0.0014
-
 VVYPWTQRY pH 8.0, 37°C Sus scrofa
3.4.24.15 0.0021
-
 LVVYPWTQRY pH 8.0, 37°C Sus scrofa
3.4.24.15 0.0026
-
 LTLRTKL pH 8.0, 37°C Sus scrofa
3.4.24.15 0.0046
-
 VVYPW-phenylThr-Gln-Arg-Tyr pH 8.0, 37°C Sus scrofa
3.4.24.15 0.0063
-
 L-phospho-Thr-Leu-Arg-Thr-Lys-Leu pH 8.0, 37°C Sus scrofa
3.4.24.16 additional information
-
 additional information peptide phosphorylation largely changes the kinetics of interaction and degredation by EP24.16 More