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3.4.17.23: angiotensin-converting enzyme 2

This is an abbreviated version!
For detailed information about angiotensin-converting enzyme 2, go to the full flat file.

Word Map on EC 3.4.17.23

Reaction

angiotensin II
+
H2O
=
angiotensin-(1-7)
+
L-phenylalanine

Synonyms

ACE, ACE 2, ACE-2, ACE-related carboxypeptidase, ACE2, ACE2 homologue, ACEH, ACEII, Ang converting enzyme 2, angiotensin converting enzyme 2, angiotensin converting enzyme II, angiotensin converting enzyme-2, angiotensin II converting enzyme 2, angiotensin-converting enzyme, angiotensin-converting enzyme 2, angiotensin-converting enzyme homolog, angiotensin-converting enzyme homologue, angiotensin-converting enzyme type 2, angiotensin-converting enzyme-2, angiotensin-converting enzyme-like protein, angiotensin-converting enzyme-related carboxypeptidase, angiotensinase, hACE2, sACE2, soluble angiotensin converting enzyme 2, TMPRSS2

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.23 angiotensin-converting enzyme 2

Crystallization

Crystallization on EC 3.4.17.23 - angiotensin-converting enzyme 2

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cryo-electron microscopy structure of ACE2 in complex with the SARS-CoV-2 Omicron variant spike protein reveals new salt bridges and hydrogen bonds formed by mutated residues Arg493, Ser496, and Arg498 in the receptor binding domain of spike protein. These interactions compensate for other Omicron mutations known to reduce ACE2 binding affinity, resulting in similar biochemical ACE2 binding affinities for the Delta and Omicron variants. Pseudoviruses that display the Omicron spike protein exhibit increased antibody evasion
crystal structure of a complex of soluble angiotensin-converting enzyme 2 (ACE2), residues 19 to 615 and SARS-CoV spike protein receptor binding domain (RBD), residues 306 to 575. Crystals in space group P21, a = 82.3 A, b = 119.4 A, c = 113.2 A, beta = 91.2°, with two complexes per asymmetric unit, are grown at room temperature from a mother liquor containing 24% polyethylene glycol 6000, 150 mM NaCl, 100 mM Tris at pH 8.2, and 10% ethylene glycol. The crystal structure at 2.9 A resolution of the RBD of the SARS-CoV spike protein bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase
hanging drop vapor diffusion at 16-18°C, crystal structures of the native and inhibitor(MLN-4760)-bound forms of the ACE2 extracellular domains are solved to 2.2 and 3.0 A resolution, respectively
hanging drop vapor diffusion at 16-18°C, crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains are solved to 2.2 A and 3.0 A resolution
interaction of ACE2 and the receptor-binding domain of SARS-CoV-2 spike protein. The omicron variant interacts with the ACE2 receptor with strong affinity involving unique amino acid residues than most of the SARS-CoV-2 variants suggesting increased infectivity and immune/vaccine evasion potential of the variant. The Lamda variant (C.37) interacts with ACE2 with higher affinity using identical receptor-binding domain residues as the omicron
modeling of the interaction with SARS-CoV-2 variants Delta plus, Iota, Kappa, Mu, Lambda, and C.1.2. Differences in the interactions between the RBD and hACE2 include hydrogen bonding, salt bridge interactions, non-bonded interactions, and binding free energy differences. All mutations in the spike protein increased the contagiousness of SARS-CoV-2 variants
molecular dynamics simulations of differently glycosylated ACE2 variants and their interaction with SARS-CoV-2 spike protein. Presence of the glycans results in stronger and longer ranged interactions that get extended by a catch-slip mechanism between the glycans. The glycans also strengthen and extend the existing protein-protein interactions
structure of the complex with SARS-CoV-2 receptor-binding domains of variants omicron and delta. The substitutions in omicron receptor-binding domian lead to changes of electrostatic charges. Compared with other variant receptor-binding domains, the binding surface of omicron receptor-binding domain has the largest-scale positive charge region. T478K, Q493R, and Q498R substitutions significantly increase positive changes, and E484A decreases the negative charges
structure of the SARS-CoV-2 chimeric receptor binding domain with human ACE2 complex. Residues Ser19, Gln24, Thr27, Phe28, His34, Glu35, Asp38, Tyr41, Gln42, Leu45, Tyr83, Asn330, Lys353, Gly354, Asp355, and Arg357 have a critical role in the binding regions. SARS-CoV has relatively similar interaction binding sites to SARS-CoV-2 except for Ser19, Leu45, Leu79, Gln325, Gly326, and Glu329 which are not involved in the interaction in SARS-CoV-2
the SARS-CoV-2 S/receptor-binding domain binding interface with ACE2 contains in total 17 residues of receptor-binding domain and 16 residues of ACE2 as interfacial residues in the protein-protein complex, forming H-bond, one salt bridge, and several van der Waals interactions. The receptor-binding domain of the spike protein has the highest affinity towards ACE2 in comparison to its two inhibitors B38 monoclonal antibody followed by Ty1 alpaca nanobody