show all | hide all No of entries

Information on EC 3.4.15.1 - peptidyl-dipeptidase A and Organism(s) Drosophila melanogaster and UniProt Accession Q10714

for references in articles please use BRENDA:EC3.4.15.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.15 Peptidyl-dipeptidases
                3.4.15.1 peptidyl-dipeptidase A
Specify your search results
Select one or more organisms in this record:
This record set is specific for:
Drosophila melanogaster
UNIPROT: Q10714 not found.
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Drosophila melanogaster
Reaction Schemes
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, angiotensin 1 converting enzyme, angiotensin converting enzyme, angiotensin converting enzyme 1, angiotensin converting enzyme I, angiotensin converting enzyme inhibitor, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
angiotensin 1 converting enzyme
-
-
-
-
angiotensin converting enzyme
-
-
-
-
angiotensin I-converting enzyme
angiotensin-converting enzyme
carboxycathepsin
-
-
-
-
carboxypeptidase, dipeptidyl
-
-
-
-
CD143 antigen
-
-
-
-
DCP
-
-
-
-
Dipeptidyl carboxypeptidase
-
-
-
-
dipeptidyl carboxypeptidase I
-
-
-
-
endothelial cell peptidyl dipeptidase
-
-
-
-
kininase II
-
-
-
-
PDH
-
-
-
-
peptidase P
-
-
-
-
peptidyl dipeptidase
-
-
-
-
peptidyl dipeptidase A
-
-
-
-
peptidyl dipeptidase I
-
-
-
-
peptidyl dipeptidase-4
-
-
-
-
peptidyl dipeptide hydrolase
-
-
-
-
peptidyl-dipeptide hydrolase
-
-
-
-
peptidyldipeptide hydrolase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9015-82-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
additional information
?
-
AnCE is a single domain protein with ACE activity, an ACE homologue
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Q10714
AnCE is a single domain protein with ACE activity, an ACE homologue
-
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
-
(2S)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
-
lisW-S
-
lisinopril-tryptophan S-enantiomer, a C-domain human sACE specific inhibitor and antihypertensive drug
perindoprilat
-
-
RXP407
-
i.e. Ac-Asp-L-Phe(PO2CH2)-L-Ala-Ala-NH2, a human sACE domain-specific phosphinic peptidyl inhibitor and antihypertensive drug
RXPA380
-
i.e. (2S)-2-[([2-[(1R)-1-[((benzyloxy)carbonyl)amino]-2-(phenylethyl)(hydroxyl)-phosphinyl]cyclopentyl]carbonyl)amino]-3-(1H-indo-3-yl)-propionic acid (Cbz-PhePSI[P(O)(OH)CH]Pro-Trp-OH), a human sACE domain-specific phosphinic peptidyl inhibitor and antihypertensive drug
trandolaprilat
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.468
hippuryl-His-Leu
-
pH 7.5, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00012
(2R)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
C-catalytic domain of ACE, pH 7.5, temperature not specified in the publication
0.000024
(2S)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
C-catalytic domain of ACE, pH 7.5, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
ACE_DROME
615
0
70914
Swiss-Prot
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystal structure of AnCE in complex with (2S)-2-({3-[hydroxyl (2-phenyl-(1R)-1-{[(benzyloxy) carbonyl]-amino}ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl}amino)-3-(4-hydroxy-phenyl) propanoic acid and (2R)-2-({3-[hydroxyl (2-phenyl-(1R)-1-{[(benzyloxy) carbonyl]-amino}ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl}amino)-3-(4-hydroxy-phenyl) propanoic acid are determined to a resolution of 1.8 and 2.0 A, respectively
-
purified recombinant free AnCE and in complex with six antihypertensive drugs, captopril, enalaprilat, lisinopril, ramiprilat, trandolaprilat, perindoprilat, lisW-S, RXPA380, and RXP407, hanging drop vapour diffusion method at 16 °C, 0.002 ml of protein solution containing 10 mg/ml native AnCE in 5 mM HEPES, pH 7.5, 0.1 mM PMSF, and 0.01 mM zinc acetate, are mixed with 0.002 ml of reservoir solution containing 0.1 M HEPES, pH 7.5, and 1.5 M sodium citrate, for enzyme complexes, the crystals are mixed with inhibitor solution, X-ray diffraction structue determination and analysis at 1.85-2.10 A resolution
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Pichia pastoris by hydrophobic interaction chromatography and gel filtration to homogeneity
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
AnCE is cloned and expressed in Pichia pastoris
-
expression in Pichia pastoris
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akif, M.; Georgiadis, D.; Mahajan, A.; Dive, V.; Sturrock, E.D.; Isaac, R.E.; Acharya, K.R.
High-resolution crystal structures of Drosophila melanogaster angiotensin-converting enzyme in complex with novel inhibitors and antihypertensive drugs
J. Mol. Biol.
400
502-517
2010
Drosophila melanogaster, Drosophila melanogaster (Q10714)
Manually annotated by BRENDA team
Masuyer, G.; Akif, M.; Czarny, B.; Beau, F.; Schwager, S.L.; Sturrock, E.D.; Isaac, R.E.; Dive, V.; Acharya, K.R.
Crystal structures of highly specific phosphinic tripeptide enantiomers in complex with the angiotensin-I converting enzyme
FEBS J.
281
943-956
2014
Drosophila melanogaster (Q10714), Homo sapiens, Homo sapiens (P12821)
Manually annotated by BRENDA team
Select items on the left to see more content.