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Literature summary 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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.15.1 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

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

Organism

EC Number Organism UniProt Comment Textmining
3.4.15.1 Homo sapiens P12821
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.4.15.1 sACE
-
 Homo sapiens
3.4.15.1 somatic ACE
-
 Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.15.1 0.004
-
 angiotensin II C-terminal domain of sACE, pH 7.5, temperature not specified in the publication Homo sapiens
3.4.15.1 0.076
-
 angiotensin II N-terminal domain of sACE, pH 7.5, temperature not specified in the publication Homo sapiens