EC number:3.4.17.23

Enzyme

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     3. Hydrolases
        3.4 Acting on peptide bonds (peptidases)
            3.4.17 Metallocarboxypeptidases
ID:3.4.17.23
Description:Angiotensin-converting enzyme 2.
Alternative Name: Angiotensin converting enzyme-2.
Angiotensin converting enzyme 2.
ACE2.
Prosite: PDOC00129;
PDB:
PDBScop

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.4.17.23
BRENDA Enzyme Link: BRENDA 3.4.17.23
KEGG Enzyme Link: KEGG3.4.17.23
BioCyc Enzyme Link: BioCyc 3.4.17.23
ExPASy Enzyme Link: ExPASy3.4.17.23
EC2PDB Enzyme Link: EC2PDB 3.4.17.23
ExplorEnz Enzyme Link: ExplorEnz 3.4.17.23
PRIAM enzyme-specific profiles Link: PRIAM 3.4.17.23
IntEnz Enzyme Link: IntEnz 3.4.17.23
MEDLINE Enzyme Link: MEDLINE 3.4.17.23

EC number:3.4.17.23

MSA:

3.4.17.23;
Phylogenetic Tree:

3.4.17.23;
Uniprot:
M-CSA:
RHEA:26554 angiotensin II + H2O = angiotensin-(1-7) + L-phenylalanine
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[NH2;+0:4]
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References

TitleAuthorsDatePubMed ID
Angiotensin-converting enzyme 2 and new insights into the renin-angiotensin system.Lambert DW, Hooper NM, Turner AJ2008 Feb 1517897633
ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.Towler P, Staker B, Prasad SG, Menon S, Tang J, Parsons T, Ryan D, Fisher M, Williams D, Dales NA, Patane MA, Pantoliano MW2004 Apr 2314754895
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, Nichols A, Tummino P2002 Apr 2611815627