EC Number   |
Reference |
|---|
   3.4.15.1 | 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 |
653341 |
| 3.4.15.1 | 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 |
731803 |
| 3.4.15.1 | 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 |
732909 |
| 3.4.15.1 | crystal structure of the N domain of human somatic angiotensin I-converting enzyme both in the presence and absence of the antihypertensive drug lisinopril |
681376 |
| 3.4.15.1 | 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 |
731803 |
| 3.4.15.1 | hanging drop method, crystal structure at a resolution of 2.25 A of testis enzyme with the highly C-domain-specific phosphinic inhibitor, RXPA380 |
678279 |
| 3.4.15.1 | hanging drop vapour diffusion method, in 10 mM sodium acetate (pH 4.7), 15% PEG 4000, and 0.01 mM ZnSO4, at 16°C |
696268 |
| 3.4.15.1 | 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 |
709546 |
| 3.4.15.1 | 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 |
707443 |
| 3.4.15.1 | 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 |
764572 |
