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Literature summary for 3.4.15.1 extracted from

  • Masuyer, G.; Schwager, S.L.; Sturrock, E.D.; Isaac, R.E.; Acharya, K.R.
    Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides (2012), Sci. Rep., 2, 717.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of human C-domain sACE in complex with two natural peptides, angiotensin II, and with a snake venom inhibitor-bradykinin potentiating peptide (BPPb, a human C-domain specific peptide inhibitor) is shown. The structure of the complex with BPPb reveals molecular interactions in a zinc independent manner. The structure of the C-domain sACE-angiotensin II complex reveals the role of the penultimate Pro residue of angiotensin II in conferring resistance to hydrolysis Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
angiotensin II angiotensin II shows selective competitive inhibition of the carboxy-terminal domain of human somatic ACE Homo sapiens
bradykinin potentiating peptide b interaction with sACE in a Zn-dependent manner Homo sapiens
captopril
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P12821
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hippuryl-L-His-L-Leu + H2O
-
 Homo sapiens hippuric acid + L-His-L-Leu
-
 ?

Synonyms

Synonyms Comment Organism
sACE
-
 Homo sapiens
somatic ACE
-
 Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.004
-
 angiotensin II C-terminal domain of sACE, pH 7.5, temperature not specified in the publication Homo sapiens
0.076
-
 angiotensin II N-terminal domain of sACE, pH 7.5, temperature not specified in the publication Homo sapiens