Preferred Label : Peptidyl-Dipeptidase A;
MeSH definition : A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc,
when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is
generally membrane-bound and active at neutral pH. It may also have endopeptidase
activity on some substrates. (From Enzyme Nomenclature, 1992) EC 3.4.15.1.; A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc,
when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is
generally membrane-bound and active at neutral pH. It may also have endopeptidase
activity on some substrates. (From Enzyme Nomenclature, 1992); A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, oligopeptide-
-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of
ANGIOTENSIN I to ANGIOTENSIN II, with increase in vasoconstrictor activity, but no
action on angiotensin II. It is also able to inactivate BRADYKININ, a potent vasodilator;
and has a glycosidase activity which releases GPI-anchored proteins from the membrane
by cleaving the mannose linkage in the GPI moiety. (From https://www.uniprot.org April
15, 2020); A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, oligopeptide-
-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of
ANGIOTENSIN I to ANGIOTENSIN II, with increase in vasoconstrictor activity, but no
action on angiotensin II. It is also able to inactivate BRADYKININ, a potent vasodilator;
and has a glycosidase activity which releases GPI-anchored proteins from the membrane
by cleaving the mannose linkage in the GPI moiety. (From https://www.uniprot.org April
15, 2020).; A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, oligopeptide--Xaa-Yaa,
when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of ANGIOTENSIN
I to ANGIOTENSIN II, with increase in vasoconstrictor activity, but no action on angiotensin
II. It is also able to inactivate BRADYKININ, a potent vasodilator; and has a glycosidase
activity which releases GPI-anchored proteins from the membrane by cleaving the mannose
linkage in the GPI moiety. (From https://www.uniprot.org April 15, 2020).;
MeSH synonym : kininase ii; carboxycathepsin; cd143 antigens; Angiotensin I-Converting Enzyme; angiotensin i converting enzyme; Kininase A; dipeptidyl peptidase a; antigens, cd143; Angiotensin Converting Enzyme; peptidyl dipeptidase A; ACE1 Protein; ACE1 Angiotensin-Converting Enzyme 1; ACE1 Angiotensin Converting Enzyme 1; Angiotensin Converting Enzyme 1; Peptidase P; Dipeptidyl Carboxypeptidase I; Carboxypeptidase I, Dipeptidyl;
Registry Number MeSH : EC 3.4.15.1;
MeSH annotation : /antag ANGIOTENSIN-CONVERTING ENZYME INHIBITORS;
Is substance : O;
UNII : EC 3.4.15.1;
Origin ID : D007703;
UMLS CUI : C0022709;
Allowable qualifiers
- Automatic exact mappings (from CISMeF team)
- Currated CISMeF NLP mapping
- False automatic mappings
- Indexing information
- Record concept(s)
- Related MeSH Supplementary Concept(s)
- Related MeSH term(s)
- Semantic type(s)
- UMLS correspondences (same concept)
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc,
when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is
generally membrane-bound and active at neutral pH. It may also have endopeptidase
activity on some substrates. (From Enzyme Nomenclature, 1992) EC 3.4.15.1.
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc,
when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is
generally membrane-bound and active at neutral pH. It may also have endopeptidase
activity on some substrates. (From Enzyme Nomenclature, 1992)
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, oligopeptide-
-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of
ANGIOTENSIN I to ANGIOTENSIN II, with increase in vasoconstrictor activity, but no
action on angiotensin II. It is also able to inactivate BRADYKININ, a potent vasodilator;
and has a glycosidase activity which releases GPI-anchored proteins from the membrane
by cleaving the mannose linkage in the GPI moiety. (From https://www.uniprot.org April
15, 2020)
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, oligopeptide-
-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of
ANGIOTENSIN I to ANGIOTENSIN II, with increase in vasoconstrictor activity, but no
action on angiotensin II. It is also able to inactivate BRADYKININ, a potent vasodilator;
and has a glycosidase activity which releases GPI-anchored proteins from the membrane
by cleaving the mannose linkage in the GPI moiety. (From https://www.uniprot.org April
15, 2020).
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, oligopeptide--Xaa-Yaa,
when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of ANGIOTENSIN
I to ANGIOTENSIN II, with increase in vasoconstrictor activity, but no action on angiotensin
II. It is also able to inactivate BRADYKININ, a potent vasodilator; and has a glycosidase
activity which releases GPI-anchored proteins from the membrane by cleaving the mannose
linkage in the GPI moiety. (From https://www.uniprot.org April 15, 2020).
https://rmlg.uliege.be/article/3385
2020
false
false
false
Belgium
coronavirus infections
pneumonia, viral
cell physiological phenomena
biochemical phenomena
Angiotensin-converting Enzyme 2 Pathway
journal article
pandemics
renin-angiotensin system
Renin-Angiotensin-Aldosterone system
Peptidyl-Dipeptidase A
pandemics
COVID-19
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