General Information:

Id: 2,069
Diseases: Diabetes mellitus, type II - [OMIM]
Insulin resistance
Homo sapiens
article
Reference: Rousseau A et al.(1995) The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme. J. Biol. Chem. 270: 3656-3661 [PMID: 7876104]

Interaction Information:

Comment Angiotensin I-converting enzyme (ACE) is a zinc-dipeptidyl carboxypeptidase, which contains two similar domains, each possessing a functional active site. Respective involvement of each active site in the degradation of the circulating peptide N-acetyl-seryl-aspartyl-lysyl-proline (AcSDKP), a negative regulator of hematopoietic stem cell proliferation, was studied by using wild-type recombinant ACE and two full-length mutants containing a single functional site. Both the N- and C-active sites of ACE exhibit dipeptidyl activity toward AcSDKP, , the N-active site hydrolyzes the peptide 50 times faster compared with the C-active site.
Formal Description
Interaction-ID: 16661

gene/protein

ACE

decreases_quantity of

gene/protein

AcSDKP

Drugbank entries Show/Hide entries for ACE
Comment Angiotensin I-converting enzyme (ACE) is a zinc-dipeptidyl carboxypeptidase, which contains two similar domains, each possessing a functional active site. Respective involvement of each active site in the degradation of the circulating peptide N-acetyl-seryl-aspartyl-lysyl-proline (AcSDKP), a negative regulator of hematopoietic stem cell proliferation, was studied by using wild-type recombinant ACE and two full-length mutants containing a single functional site. Both the N- and C-active sites of ACE exhibit dipeptidyl activity toward AcSDKP, , the N-active site hydrolyzes the peptide 50 times faster compared with the C-active site.
Formal Description
Interaction-ID: 16662

gene/protein

ACE

increases_quantity of

drug/chemical compound

Lys-Pro

Drugbank entries Show/Hide entries for ACE
Comment Angiotensin I-converting enzyme (ACE) is a zinc-dipeptidyl carboxypeptidase, which contains two similar domains, each possessing a functional active site. Respective involvement of each active site in the degradation of the circulating peptide N-acetyl-seryl-aspartyl-lysyl-proline (AcSDKP), a negative regulator of hematopoietic stem cell proliferation, was studied by using wild-type recombinant ACE and two full-length mutants containing a single functional site. Both the N- and C-active sites of ACE exhibit dipeptidyl activity toward AcSDKP, , the N-active site hydrolyzes the peptide 50 times faster compared with the C-active site.
Formal Description
Interaction-ID: 16734

gene/protein

ACE

increases_quantity of

drug/chemical compound

Ac-Ser-Asp

Drugbank entries Show/Hide entries for ACE