Enzymes
| UniProtKB help_outline | 6 proteins |
Reaction participants Show >> << Hide
- Name help_outline dynorphin A-(1-13) Identifier CHEBI:147381 Charge 5 Formula C75H131N24O15 InChIKeyhelp_outline OVVIBUHLQIYUEU-IWIISZHXSA-S SMILEShelp_outline C([C@H](CCCC[NH3+])NC([C@H](CC(C)C)NC([C@H](CCCC[NH3+])NC(=O)[C@H]1N(CCC1)C([C@H](CCCNC(=[NH2+])N)NC([C@H]([C@H](CC)C)NC([C@H](CCCNC(=[NH2+])N)NC([C@H](CCCNC(=[NH2+])N)NC([C@H](CC(C)C)NC([C@H](CC2=CC=CC=C2)NC(=O)CNC(=O)CNC([C@H](CC3=CC=C(C=C3)O)[NH3+])=O)=O)=O)=O)=O)=O)=O)=O)=O)(=O)[O-] 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 (Beilstein: 3587155; 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 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dynorphin A-(1-12) Identifier CHEBI:147383 Charge 4 Formula C69H118N22O14 InChIKeyhelp_outline RPMUYLYFDVEEGF-XLWMICEOSA-R SMILEShelp_outline [O-]C([C@H](CC(C)C)NC([C@H](CCCC[NH3+])NC(=O)[C@H]1N(CCC1)C([C@H](CCCNC(=[NH2+])N)NC([C@H]([C@H](CC)C)NC([C@H](CCCNC(=[NH2+])N)NC([C@H](CCCNC(=[NH2+])N)NC([C@H](CC(C)C)NC([C@H](CC2=CC=CC=C2)NC(=O)CNC(=O)CNC([C@H](CC3=CC=C(C=C3)O)[NH3+])=O)=O)=O)=O)=O)=O)=O)=O)=O 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 L-lysine Identifier CHEBI:32551 Charge 1 Formula C6H15N2O2 InChIKeyhelp_outline KDXKERNSBIXSRK-YFKPBYRVSA-O SMILEShelp_outline [NH3+]CCCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 65 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:63556 | RHEA:63557 | RHEA:63558 | RHEA:63559 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase.
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
Human angiotensin-converting enzyme-related carboxypeptidase (ACE2) is a zinc metalloprotease whose closest homolog is angiotensin I-converting enzyme. To begin to elucidate the physiological role of ACE2, ACE2 was purified, and its catalytic activity was characterized. ACE2 proteolytic activity h ... >> More
Human angiotensin-converting enzyme-related carboxypeptidase (ACE2) is a zinc metalloprotease whose closest homolog is angiotensin I-converting enzyme. To begin to elucidate the physiological role of ACE2, ACE2 was purified, and its catalytic activity was characterized. ACE2 proteolytic activity has a pH optimum of 6.5 and is enhanced by monovalent anions, which is consistent with the activity of ACE. ACE2 activity is increased approximately 10-fold by Cl(-) and F(-) but is unaffected by Br(-). ACE2 was screened for hydrolytic activity against a panel of 126 biological peptides, using liquid chromatography-mass spectrometry detection. Eleven of the peptides were hydrolyzed by ACE2, and in each case, the proteolytic activity resulted in removal of the C-terminal residue only. ACE2 hydrolyzes three of the peptides with high catalytic efficiency: angiotensin II () (k(cat)/K(m) = 1.9 x 10(6) m(-1) s(-1)), apelin-13 (k(cat)/K(m) = 2.1 x 10(6) m(-1) s(-1)), and dynorphin A 1-13 (k(cat)/K(m) = 3.1 x 10(6) m(-1) s(-1)). The ACE2 catalytic efficiency is 400-fold higher with angiotensin II () as a substrate than with angiotensin I (). ACE2 also efficiently hydrolyzes des-Arg(9)-bradykinin (k(cat)/K(m) = 1.3 x 10(5) m(-1) s(-1)), but it does not hydrolyze bradykinin. An alignment of the ACE2 peptide substrates reveals a consensus sequence of: Pro-X((1-3 residues))-Pro-Hydrophobic, where hydrolysis occurs between proline and the hydrophobic amino acid. << Less
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [EuropePMC]
This publication is cited by 7 other entries.