3.4.15.1: peptidyl-dipeptidase A
This is an abbreviated version!
For detailed information about peptidyl-dipeptidase A, go to the full flat file.
Word Map on EC 3.4.15.1
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3.4.15.1
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hypertension
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blocker
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cardiovascular
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arterial
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antihypertensive
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cardiac
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renin-angiotensin
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ventricular
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myocardial
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captopril
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systolic
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diuretic
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coronary
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renin
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aceis
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infarction
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beta-blockers
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enalapril
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glomerular
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diastolic
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ejection
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proteinuria
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mellitus
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placebo
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hypertrophy
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aldosterone
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nephropathy
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creatinine
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hemodynamic
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bradykinin
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congestive
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ras
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vasodilator
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normotensive
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statin
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renin-angiotensin-aldosterone
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hg
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sarcoidosis
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losartan
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aspirin
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prescript
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double-blind
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angiotensinogen
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renoprotective
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pressor
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digoxin
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all-cause
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renovascular
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microalbuminuria
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hypotensive
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drug development
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veterinary medicine
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medicine
- 3.4.15.1
- hypertension
-
blocker
- cardiovascular
- arterial
-
antihypertensive
- cardiac
-
renin-angiotensin
- ventricular
- myocardial
- captopril
-
systolic
-
diuretic
- coronary
- renin
-
aceis
- infarction
-
beta-blockers
- enalapril
- glomerular
-
diastolic
-
ejection
- proteinuria
- mellitus
-
placebo
- hypertrophy
- aldosterone
- nephropathy
- creatinine
-
hemodynamic
- bradykinin
-
congestive
- ras
-
vasodilator
-
normotensive
- statin
-
renin-angiotensin-aldosterone
- hg
- sarcoidosis
- losartan
- aspirin
-
prescript
-
double-blind
- angiotensinogen
-
renoprotective
-
pressor
- digoxin
-
all-cause
-
renovascular
-
microalbuminuria
-
hypotensive
- drug development
- veterinary medicine
- medicine
Reaction
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 =
Synonyms
ACE, ACE-1, ACE2, ACEI, ANCE, ANG I-converting enzyme, angiotensin 1 converting enzyme, angiotensin converting enzyme, angiotensin converting enzyme 1, angiotensin converting enzyme I, angiotensin converting enzyme inhibitor, angiotensin I converting enzyme, angiotensin I-converting enzyme, angiotensin-converting enzyme, angiotensin-converting enzyme 2, angiotensin-converting enzyme type 1, angiotensin-converting enzyme-2, angiotensin-converting-enzyme, angiotensin-I converting enzyme, angiotensin-I-converting enzyme, carboxycathepsin, carboxypeptidase, dipeptidyl, CD143, CD143 antigen, crab-ACE, DCP, Dcp1, Dipeptidyl carboxypeptidase, dipeptidyl carboxypeptidase I, dipeptidylcarboxypeptidase, endothelial cell peptidyl dipeptidase, gACE, germinal ACE, kinases II peptidyldipeptide hydrolase, kininase II, mACE2, More, PDH, peptidase P, peptidyl dipeptidase, peptidyl dipeptidase A, peptidyl dipeptidase I, peptidyl dipeptidase-4, peptidyl dipeptide hydrolase, peptidyl-dipeptide hydrolase, peptidyldipeptide hydrolase, rhACE2, s-ACE, sACE, sACE-1, somatic ACE, somatic angiotensin I-converting enzyme, TACE, testicular ACE, testis ACE, XcACE, zinc dipeptidyl carboxypeptidase, Zn2+ peptidyldipeptidase
ECTree
3.4.15.1 peptidyl-dipeptidase AAdvanced search results
results (
results (Engineering
Engineering on EC 3.4.15.1 - peptidyl-dipeptidase A
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D377Q
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
D453E
E162D
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
E376D
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
E403R
the mutation does not contribute individually to C domain-selective inhibitor binding
F391Y
K1087A
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no activity with angiotensin I, kcat/KM for [Phe9]angiotensin I is 654fold lower than wild-type value, kcat/KM for [Arg10]angiotensin I is 193fold lower than wild-type value, kcat/KM for [Phe9,Arg10]angiotensin I is 462fold lower than wild-type value
L19E
the mutation alters the binding of monoclonal antibodies to the N domain of ACE and shedding of ACE domains
Q18H
the mutation alters the binding of monoclonal antibodies to the N domain of ACE and shedding of ACE domains
Q22A
the mutation alters the binding of monoclonal antibodies to the N domain of ACE and shedding of ACE domains
R1098Q
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kcat/KM for angiotensin I is 7fold lower than wild-type value, kcat/KM for [Phe9]angiotensin I is 2.2fold higher than wild-type value, kcat/KM for [Arg10]angiotensin I is 23fold lower than wild-type value, kcat/KM for [Phe9,Arg10]angiotensin I is 1.4fold lower than wild-type value
S516N
the S516N substitution results in a inhibitor binding affinity comparable to that of the wild type C domain
T282S
V379/V380T
the mutation displays small decrease in affinity for inhibitor (5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
V379S
V380T
V518T
Y1096F
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kcat/KM for angiotensin I is 12fold lower than wild-type value, kcat/KM for [Phe9]angiotensin I is 8.9fold lower than wild-type value, kcat/KM for [Arg10]angiotensin I is 8.5fold lower than wild-type value, kcat/KM for [Phe9,Arg10]angiotensin I is 7fold lower than wild-type value
Y1096F/K1087A
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no activity with angiotensin I, [Phe9]angiotensin I, [Arg10]angiotensin I, and [Phe9,Arg10]angiotensin I
S730A
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cleavage secretion of the mutant angiotensin-converting enzyme remains susceptible to the enhancing effect of phorbol 12-myristate 13-acetate and calmodulin inhibitor CaMI
additional information
D453E
the mutation does not contribute individually to C domain-selective inhibitor binding
D453E
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
F391Y
the F391Y mutation in the S2 pocket causes an 8fold decrease in inhibitor affinity relative to the wild type C domain
F391Y
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
T282S
the mutation does not contribute individually to C domain-selective inhibitor binding
T282S
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
V379S
the mutation does not contribute individually to C domain-selective inhibitor binding
V379S
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
V380T
the mutation displays small decrease in affinity for inhibitor (5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
V380T
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
V518T
the mutation shows the greatest decrease in affinity for inhibitor (5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
V518T
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
additional information
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mutants K361,365 and mutant K961,963, in which one active site has been inactivated by site-directed mutagenesis. Both active centers are catalytically active in the cell membrane-anchored enzyme and convert angiotensin I to angiotensin II
additional information
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substrate specificity characterization of two full-length mutant enzymes with either the N or C catalytic site inactivated by substitution of the two zinc-binding His by Lys (referred as N- or C-domains)
additional information
regions of the testis ACE sequence are replaced with the corresponding N-domain sequence. The resultant chimeras C1-163Ndom-ACE, C417-579Ndom-ACE, and C583-623Ndom-ACE are processed to the cell surface of transfected Chinese hamster ovary cells, and are cleaved at the identical site as that of tACE. They show acquisition of N-domain-like catalytic properties. Homology modelling of the chimeric proteins reveals structural changes in regions required for tACE-specific catalytic activity. In contrast, C164-416Ndom-ACE and C191-214Ndom-ACE demonstrate defective intracellular processing and are neither enzymatically active nor shed. Therefore, critical elements within region D164V416 and more specifically I191T214 are required for the processing, cell-surface targeting, and enzyme activity of tACE, and cannot be substituted for by the homologous N-domain sequence
additional information
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ACE insertion/deletion and bradykinin B2 receptor polymorphisms are not involved in the development of ACEi-induced angio-oedema, ACE insertion/deletion polymorphism identification and analysis, overview
additional information
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angiotensin-converting enzyme gene polymorphisms among Saudi population from Qassim region, genotyping, overview
additional information
construction of a minimally glycosylated tACE mutant, tACE-G13, truncated after Ser625 and lacking 36 O-glycosylated N-terminal residues as well as all but two N-glycosylation sites. Mutation of C-domain-specific active-site residues to their N-domain equivalents
additional information
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construction of a minimally glycosylated tACE mutant, tACE-G13, truncated after Ser625 and lacking 36 O-glycosylated N-terminal residues as well as all but two N-glycosylation sites. Mutation of C-domain-specific active-site residues to their N-domain equivalents
additional information
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influence of ACE gene insertion/deletion polymorphisms, rs1799752, D-and I-alleles, on ACE inhibitor effects in treatment of heart failure, comparison to effects of polymorphisms of angiotensionogen gene, i.e. T174M, M235T, G6A, A20C, G152A, and G217A, and of the A1166C polymorphisms of the angiotensin II type I receptor, overview. The genetic variants in the renin-angiotensin system genes are associated with long-term mortality and cardiovascular events in the patients with diastolic heart failure, but can be modified by the use of ACE inhibitors
additional information
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polymorphism of ACE insertion/deletion, e.g. cC181T, and the bradykinin B2 receptor polymorphisms are not involved in the development of ACEi-induced angioedema, overview
additional information
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autonomic dysregulation in ob/ob mice is improved by inhibition of angiotensin-converting enzyme
additional information
generation of genetically engineered mice carrying a duplication of the ACE gene on chromosome 11 on a C57Bl6/J background, the littermate mice carry three (heterozygote for the duplication) functional ACE gene copies. Phenotype and regulatory effects of the mutation, overview
additional information
lentivirus-mediated shRNA knockdown of somatic ACE, sAce
additional information
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lentivirus-mediated shRNA knockdown of somatic ACE, sAce
additional information
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generation of genetically engineered mice carrying a duplication of the ACE gene on chromosome 11 on a C57Bl6/J background, the littermate mice carry three (heterozygote for the duplication) functional ACE gene copies. Phenotype and regulatory effects of the mutation, overview
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