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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

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 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.15 Peptidyl-dipeptidases
                3.4.15.1 peptidyl-dipeptidase A

Crystallization

Crystallization on EC 3.4.15.1 - peptidyl-dipeptidase A

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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
angiotensin-converting enzyme-lisinopril complex, 2.0 A resolution, vapour diffusion method. The structure provides an opportunity to design domain-selective ACE inhibitors that may exhibit new pharmacological profiles
crystal structure of human C-domain sACE in complex with two natural peptides, angiotensin II, and with a snake venom inhibitor-bradykinin potentiating peptide (BPPb, a human C-domain specific peptide inhibitor) is shown. The structure of the complex with BPPb reveals molecular interactions in a zinc independent manner. The structure of the C-domain sACE-angiotensin II complex reveals the role of the penultimate Pro residue of angiotensin II in conferring resistance to hydrolysis
crystal structure of the N domain of human somatic angiotensin I-converting enzyme both in the presence and absence of the antihypertensive drug lisinopril
crystal structures of the two catalytic domains of human ACE (N- and C-) 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 1.91 and 1.85 A, respectively
hanging drop method, crystal structure at a resolution of 2.25 A of testis enzyme with the highly C-domain-specific phosphinic inhibitor, RXPA380
hanging drop vapour diffusion method, in 10 mM sodium acetate (pH 4.7), 15% PEG 4000, and 0.01 mM ZnSO4, at 16°C
purified recombinant mutant tACE-G13 in complex with inhibitor lisW-S, microseeding, 1.45 mg/ml tACE-G13 with 0.250 mM lisW-S over precipitant solution comprising 15% w/v PEG 4000, 0.010 mM ZnSO4, and 10 mM sodium acetate, pH 4.7, 2 weeks, X-ray diffraction structure determination and analysis at 2.3 A resolution, modelling
structures of full-length, glycosylated sACE in monomeric and dimeric forms. The N- and C-terminal domains of monomeric sACE are resolved at 3.7 and 4.1A, respectively, the interacting N-terminal domains responsible for dimer formation at 3.8 A. The sACE monomer domains interact and are in an open conformation. The open N-domain active site is primed for substrate binding to the zinc site and the catalytic anchor residues Q259, K489, and Y498. sACE homodimerization occurs via the N-domain and increases flexibility at the allosteric site, formed by three C-terminal loops
vapour-diffusion hanging-drop method, wild-type and underglycosylated mutant enzymes. The truncated soluble enzyme DELTA1-36, expressed in the presence of the glucosidase-I inhibitor N-butyldeoxynojirimycin, retains the activity of the native enzyme and yields crystals belongining to the orthorhombic P2(1)2(1)2(1) space group. Cell dimensions: a = 56.47 A, b = 84.9 A, c = 144.99 A, alpha = 90°, beta = 90° and gamma = 90°
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X-ray crystal structure of tACE and its complex with the inhibitor lisinopril. The structure of tACE is mainly helical with a central cavity or channel that extends for about 30 A into the molecule
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