General Information:

Id: 2,074 (click here to show other Interactions for entry)
Diseases: Diabetes mellitus, type II - [OMIM]
Insulin resistance
Homo sapiens
article
Reference: Hayakari M et al.(1997) Kinetic evaluation of beta-neoendorphin hydrolysis by the somatic and testicular isozymes of human angiotensin-converting enzyme. Biochim. Biophys. Acta 1339: 31-38 [PMID: 9165097]

Interaction Information:

Comment Angiotensin-converting enzyme (ACE) has both somatic and testicular isozymes, the former possessing two catalytically active domains, amino-terminal and carboxyl-terminal, while the latter has only the carboxyl-terminal one. Hydrolysis of beta-neoendorphin(1-9) by both the somatic and testicular isozymes (ACE-S and ACE-T) proceeds by the sequential removal of carboxyl-terminal dipeptides in three consecutive steps: beta-neoendorphin(1-9) is cleaved to beta-neoendorphin(1-7) plus Tyr-Pro, beta-neoendorphin(1-7) is cleaved to Leu-enkephalin plus Arg-Lys, Leu-enkephalin is cleaved to Tyr-Gly-Gly plus Phe-Leu.
Formal Description
Interaction-ID: 16731

gene/protein

ACE

decreases_quantity of

gene/protein

Leu-enkephalin

Drugbank entries Show/Hide entries for ACE