Literature summary for 3.4.15.1 extracted from

Lubbe, L.; Sewell, B.T.; Woodward, J.D.; Sturrock, E.D.
Cryo-EM reveals mechanisms of angiotensin I-converting enzyme allostery and dimerization (2022), EMBO J., 41, e110550 .

Activating Compound

Activating Compound	Comment	Organism	Structure
Cl-	assay in the presence of zinc and chloride	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
expression in CHO-K1 cells	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Homo sapiens

Crystallization (Comment)

Organism

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

Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	assay in the presence of zinc and chloride	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
244000	-	gel filtration	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P12821	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	modeling of a biantennary fucosylated complex-type glycan structure into cryo-EM maps	Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
49.09	-	pH 8.3, 37°C	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Z-phenylalanyl-histidyl-leucine + H2O	-	Homo sapiens	Z-phenylalanine + histidyl-leucine	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 138000, calculated from sequence, 1 * 170000, SDS-PAGE	Homo sapiens
More	the protein seems mostly monomeric in solution, but the dimer is detected in both 2D and 3D cryo-EM reconstruction	Homo sapiens

Synonyms

Synonyms	Comment	Organism
angiotensin-converting enzyme	-	Homo sapiens
sACE	-	Homo sapiens