Evaluation of the inhibition of other metalloproteinases by matrix metalloproteinase inhibitors.
J Enzyme Inhib
; 14(6): 425-35, 1999.
Article
em En
| MEDLINE
| ID: mdl-10536876
ABSTRACT
Two series of compounds synthesized as specific matrix metalloproteinase (MMP) inhibitors have been evaluated for their inhibition of non-MMPs. In a series of substituted succinyl hydroxamic acids, some were found to be significant (IC50 < 1 microM) inhibitors of leucine (microsomal) aminopeptidase, neprilysin (3.4.24.11), and thermolysin. Macrocyclic compounds in which the alpha carbon of the succinyl hydroxamate is linked to the side chain of the P2' amino acid were found to be good inhibitors of aminopeptidase, but not of neprilysin or thermolysin. Compounds of neither series were found to be significant inhibitors of angiotensin converting enzyme or carboxypeptidase A.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Metaloendopeptidases
/
Inibidores de Metaloproteinases de Matriz
Limite:
Animals
Idioma:
En
Revista:
J Enzyme Inhib
Assunto da revista:
BIOQUIMICA
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
Estados Unidos