Angiotensin-converting enzyme

1O86, 1O8A, 1UZE, 1UZF, 2C6F, 2C6N, 2IUL, 2IUX, 2OC2, 2XY9, 2XYD, 2YDM, 3BKK, 3BKL, 3NXQ, 4APH, 4APJ, 3L3N, 4BXK, 4BZR, 4BZS, 4C2N, 4C2O, 4C2P, 4C2Q, 4C2R, 4CA5, 4CA6, 4UFA, 4UFB, 5AMB, 5AM9, 5AM8, 5AMC, 5AMA163611421ENSG00000159640ENSMUSG00000020681P12821P09470NM_001382701NM_001382702NM_009598NM_207624NM_001281819NP_001369631NP_001268748NP_033728NP_997507Angiotensin-converting enzyme (EC 3.4.15.1), or ACE, is a central component of the renin–angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body.

[9] ACE is a central component of the renin–angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body.

Brain tissue has ACE enzyme, which takes part in local RAS and converts Aβ42 (which aggregates into plaques) to Aβ40 (which is thought to be less toxic) forms of beta amyloid.

ACE inhibitors that cross the blood–brain barrier and have preferentially selected N-terminal activity may therefore cause accumulation of Aβ42 and progression of dementia.

Some studies suggest that ACE inhibitors that are able to pass the blood-brain-barrier (BBB) could enhance the activity of major amyloid-beta peptide degrading enzymes like neprilysin in the brain resulting in a slower development of Alzheimer's disease.

[20] More recent research suggests that ACE inhibitors can reduce risk of Alzheimer's disease in the absence of apolipoprotein E4 alleles (ApoE4), but will have no effect in ApoE4- carriers.

It is assumed that ACE can degrade beta-amyloid in brain blood vessels and therefore help prevent the progression of the disease.

[24] Studies have shown that different genotypes of angiotensin converting enzyme can lead to varying influence on athletic performance.

The rs1799752 I/D polymorphism (aka rs4340, rs13447447, rs4646994) consists of either an insertion (I) or deletion (D) of a 287 base pair sequence in intron 16 of the gene.

Short distance swimmers show an increased frequency of the D-allele, since their discipline relies more on strength than endurance.

[30] The crystal structure of human testis ACE was solved in the year 2002 by Ramanathan Natesh in the lab of K. Ravi Acharya in collaboration with Sylva Schwager and Edward Sturrock who purified the protein.

Proposed ACE catalytic mechanism
Schematic diagram of the renin–angiotensin–aldosterone system
Anatomical diagram of the renin–angiotensin system, showing the role of ACE at the lungs [ 11 ]
ACE in complex with inhibitor lisinopril, zinc cation shown in grey, chloride anions in yellow. Based on PyMOL rendering of PDB 1o86 . The picture shows that lisinopril is a competitive inhibitor, since it and angiotensin I are similar structurally. Both bind to the active site of ACE. The structure of the ACE-lisinopril complex was confirmed by X-ray crystallography . [ 15 ]