Reaction participants Show >> << Hide
- Name help_outline bradykinin Identifier CHEBI:132988 Charge 2 Formula C50H75N15O11 InChIKeyhelp_outline QXZGBUJJYSLZLT-FDISYFBBSA-P SMILEShelp_outline C(=[NH2+])(NCCC[C@@H](C(=O)N1[C@H](C(N2[C@H](C(=O)NCC(N[C@H](C(N[C@H](C(=O)N3[C@H](C(=O)N[C@H](C(N[C@H](C([O-])=O)CCCNC(=[NH2+])N)=O)CC=4C=CC=CC4)CCC3)CO)=O)CC=5C=CC=CC5)=O)CCC2)=O)CCC1)[NH3+])N 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-Phe-L-Arg Identifier CHEBI:133147 Charge 1 Formula C15H24N5O3 InChIKeyhelp_outline OZILORBBPKKGRI-RYUDHWBXSA-O SMILEShelp_outline C(=O)([C@@H]([NH3+])CC1=CC=CC=C1)N[C@H](C(=O)[O-])CCCNC(=[NH2+])N 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline bradykinin(1-7) Identifier CHEBI:147352 Charge 1 Formula C35H53N10O9 InChIKeyhelp_outline CRROPKNGCGVIOG-QCOJBMJGSA-O SMILEShelp_outline C(=[NH2+])(NCCC[C@@H](C(=O)N1[C@H](C(N2[C@H](C(=O)NCC(N[C@H](C(N[C@H](C(=O)N3[C@H](C(=O)[O-])CCC3)CO)=O)CC=4C=CC=CC4)=O)CCC2)=O)CCC1)[NH3+])N 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:71451 | RHEA:71452 | RHEA:71453 | RHEA:71454 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Publications
-
Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides.
Jaspard E., Wei L., Alhenc-Gelas F.
Angiotensin I-converting enzyme (ACE, E.C.3.4.15.1) has been recently shown to contain two very similar domains, each of which bears a functional active site hydrolyzing Hip-His-Leu or angiotensin I (AI). The substrate specificity of the two active sites of ACE was compared using wild-type recombi ... >> More
Angiotensin I-converting enzyme (ACE, E.C.3.4.15.1) has been recently shown to contain two very similar domains, each of which bears a functional active site hydrolyzing Hip-His-Leu or angiotensin I (AI). The substrate specificity of the two active sites of ACE was compared using wild-type recombinant ACE and mutants, where one active site is suppressed by deletion or inactivated by mutations of 2 histidines coordinating an essential zinc atom. Both active sites converted bradykinin (BK) to BK1-7 and BK1-5 with similar kinetics and with Kappm at least 30 times lower and kcat/kappm 10 times higher than for AI. The carboxyl-terminal active site, but not the amino-terminal site, was activated by chloride; however, chloride activation was minimal compared with AI. Both domains also hydrolyzed substance P and cleaved a carboxyl-terminal protected dipeptide and tripeptide. The carboxyl-terminal active site was more readily activated by chloride and hydrolyzed substance P faster. Luteinizing-hormone releasing hormone was hydrolyzed by both active sites, but hydrolysis by the amino-terminal active site was faster. It performed the endoproteolytic amino-terminal cleavage of this peptide at least 30 times faster than the carboxyl-terminal active site. Both active sites cleaved a carboxyl-terminal tripeptide from luteinizing hormone-releasing hormone. Thus, both active sites of ACE possess dipeptidyl carboxypeptidase and endopeptidase activities. However, only the carboxyl-terminal active site can undergo a chloride-induced alteration that greatly enhances the hydrolysis of AI or substance P, and the amino-terminal active site possesses an unusual amino-terminal endoproteolytic specificity for a natural peptide. This suggests physiologically important differences between the subsites of the two active centers, and different substrate specificity, despite the high degree of sequence homology. << Less
-
A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin.
Yang H.Y., Erdoes E.G., Levin Y.
Biochim. Biophys. Acta 214:374-376(1970) [PubMed] [EuropePMC]
-
Second kininase in human blood plasma.
Yang H.Y., Erdoes E.G.