Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.11 (CD10)
 9,792 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The elastase of human spleen was shown to exhibit endopeptidase activity against azo-casein and elastin. 2. Activity against several synthetic substrates was detected, and benzyloxycarbonyl-L-alanine 2-naphthyl ester was found to be a good substrate for routine use. 3. The enzyme showed a broad pH optimum in the range of 8.2-9.2 against azo-casein and the synthetic substrate. 4. The effect of inhibitors on the spleen elastase showed it to be a serine proteinase with a specificity similar to that of porcine pancreatic elastase. 5. Specific antisera were raised against the enzyme, and it was shown to be immunologically identical with the lysosomal elastase of human neutrophil leucocytes.
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PMID:Human lysosomal elastase. Catalytic and immunological properties. 93 78

The structure-activity relationships of phosphoramidon analogues for inhibition of endothelin-converting enzyme (ECE), neutral endopeptidase 24.11 (NEP), and angiotensin-converting enzyme (ACE) were compared. Phosphoramidon inhibited ECE, NEP, and ACE activities with IC50 values of 3.5, 0.034, and 78 microM, respectively. Removal of the rhamnose moiety of phosphoramidon (dipeptide 3) reduced the potency for ECE (IC50 = 70 microM), whereas the potencies for NEP (0.003 microM) and ACE (0.20 microM) were increased. Addition of 2-(2-naphthyl)ethyl to dipeptide 3 improved the potency for ECE (0.55 microM) but weakened the potency for NEP (0.02 microM), and had no significant change for ACE. Interchange between Leu and Trp abolished the inhibitory activities for ECE and NEP, but the compound remained active for ACE. These results suggest that a hydrophobic group in the P1 position of phosphoramidon analogues increases the potency for ECE significantly, whereas compounds containing a free phosphonic acid are optimal for inhibition of NEP and ACE. Furthermore, an aromatic group in the P'2 position is essential for the inhibition of ECE and NEP, but not ACE.
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PMID:Differential structure-activity relationships of phosphoramidon analogues for inhibition of three metalloproteases: endothelin-converting enzyme, neutral endopeptidase, and angiotensin-converting enzyme. 858 70