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

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.15 Peptidyl-dipeptidases
                3.4.15.1 peptidyl-dipeptidase A
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This record set is specific for:
Drosophila melanogaster
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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
angiotensin-converting enzyme, angiotensin converting enzyme, angiotensin converting enzyme inhibitor, angiotensin i-converting enzyme, angiotensin-converting-enzyme, angiotensin i converting enzyme, ace-1, kininase ii, angiotensin-i converting enzyme, angiotensin-converting enzyme-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
angiotensin 1 converting enzyme
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angiotensin converting enzyme
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angiotensin I-converting enzyme
angiotensin-converting enzyme
carboxycathepsin
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-
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carboxypeptidase, dipeptidyl
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-
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CD143 antigen
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DCP
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-
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Dipeptidyl carboxypeptidase
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-
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dipeptidyl carboxypeptidase I
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endothelial cell peptidyl dipeptidase
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kininase II
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-
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PDH
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-
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peptidase P
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peptidyl dipeptidase
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peptidyl dipeptidase A
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peptidyl dipeptidase I
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peptidyl dipeptidase-4
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peptidyl dipeptide hydrolase
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peptidyl-dipeptide hydrolase
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peptidyldipeptide hydrolase
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-
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CAS REGISTRY NUMBER
COMMENTARY hide
9015-82-1
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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
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-
-
?
additional information
?
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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
?
-
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
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(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
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lisW-S
lisinopril-tryptophan S-enantiomer, a C-domain human sACE specific inhibitor and antihypertensive drug
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
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
LOCALIZATION PREDICTION?
ACER_DROME
630
0
73057
Swiss-Prot
Secretory Pathway (Reliability: 1)
ACE_DROME
615
0
70914
Swiss-Prot
Secretory Pathway (Reliability: 1)
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 (Q10714), Drosophila melanogaster
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
Homo sapiens (P12821), Homo sapiens, Drosophila melanogaster (Q10714)
Manually annotated by BRENDA team