関: angiotensin I-converting enzyme、angiotensin-converting enzyme

WordNet

the 1st letter of the Roman alphabet (同)a
the blood group whose red cells carry the A antigen (同)type_A, group A

PrepTutorEJDIC

answer / ampere
arsenicの化学記号

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/03/03 16:08:28」(JST)

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proposed ACE catalytic mechanism

Angiotensin-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. It converts the hormone angiotensin I to the active vasoconstrictor angiotensin II. Therefore, ACE indirectly increases blood pressure by causing blood vessels to constrict. ACE inhibitors are widely used as pharmaceutical drugs for treatment of cardiovascular diseases.

The enzyme was discovered by Leonard T. Skeggs Jr. in 1956.^[4] It is located mainly in the capillaries of the lungs but can also be found in endothelial and kidney epithelial cells.^[5]

Other less known functions of ACE are degradation of bradykinin^[6] and amyloid beta-protein.^[7]

Nomenclature

ACE is also known by the following names:

dipeptidyl carboxypeptidase I,
peptidase P,
dipeptide hydrolase,
peptidyl dipeptidase,
angiotensin converting enzyme,
kininase II,
angiotensin I-converting enzyme,
carboxycathepsin,
dipeptidyl carboxypeptidase,
"hypertensin converting enzyme" peptidyl dipeptidase I,
peptidyl-dipeptide hydrolase,
peptidyldipeptide hydrolase,
endothelial cell peptidyl dipeptidase,
peptidyl dipeptidase-4,
PDH,
peptidyl dipeptide hydrolase,
and DCP.

Function

Schematic diagram of the renin–angiotensin–aldosterone system

Anatomical diagram of the renin-angiotensin system, showing the role of ACE at the lungs.^[8]

ACE hydrolyzes peptides by the removal of a dipeptide from the C-terminus. Likewise it converts the inactive decapeptide angiotensin I to the octapeptide angiotensin II by removing the dipeptide His-Leu.^[9]

Angiotensin II is potent vasoconstrictor in a substrate concentration-dependent manner.^[10] Angiotensin II binds to the type 1 angiotensin II receptor (AT1), which sets off a number of actions that result in vasoconstriction and therefore increased blood pressure.

ACE is also part of the kinin-kallikrein system where it degrades bradykinin, a potent vasodilator, and other vasoactive peptides.^[11]

Kininase II is the same as angiotensin-converting enzyme. Thus, the same enzyme (ACE) that generates a vasoconstrictor (ANG II) also disposes of vasodilators (bradykinin).^[8]

Mechanism

ACE is a zinc metalloenzyme.^[12] The zinc ion is essential to its activity, since it directly participates in the catalysis of the peptide hydrolysis. Therefore, ACE can be inhibited by metal-chelating agents.^[13]

The E384 residue was found to have a dual function. First it acts as a general base to activate water as a nucleophile. Then it acts as a general acid to cleave the C-N bond.^[14]

The function of the chloride ion is very complex and is highly debated. The anion activation by chloride is a characteristic feature of ACE.^[15] It was experimentally determined that the activation of hydrolysis by chloride is highly dependent on the substrate. While it increases hydrolysis rates for e.g. Hip-His-Leu it inhibits hydrolysis of other substrates like Hip-Ala-Pro.^[14] Under physiological conditions the enzyme reaches about 60% of its maximal activity toward angiotensin I while it reaches its full activity toward bradykinin. It is therefore assumed that the function of the anion activation in ACE provides high substrate specificity.^[15] Other theories say that the chloride might simply stabilize the overall structure of the enzyme.^[14]

Genetics

The ACE gene, ACE, encodes two isozymes. The somatic isozyme is expressed in many tissues, mainly in the lung, including vascular endothelial cells, epithelial kidney cells, and testicular Leydig cells, whereas the germinal is expressed only in sperm. 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. The latter is predominantly a function of N domain portion on the ACE enzyme. 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.^{[citation needed]}

Disease relevance

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 has a similar structure to angiotensin I and binds to the active site of ACE.

ACE inhibitors are widely used as pharmaceutical drugs in the treatment of conditions such as high blood pressure, heart failure, diabetic nephropathy, and type 2 diabetes mellitus.

ACE inhibitors inhibit ACE competitively.^[16] That results in the decreased formation of angiotensin II and decreased metabolism of bradykinin, which leads to systematic dilation of the arteries and veins and a decrease in arterial blood pressure. In addition, inhibiting angiotensin II formation diminishes angiotensin II-mediated aldosterone secretion from the adrenal cortex, leading to a decrease in water and sodium reabsorption and a reduction in extracellular volume.^[17]

ACE's effect on Alzheimer's disease is still highly debated. Alzheimer patients usually show higher ACE levels in their brain. 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.^[18] 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 affect in ApoE4- carriers.^[19] Another more recent hypothesis is that higher levels of ACE can prevent Alzheimer's. It is assumed that ACE can degrade beta-amyloid in brain blood vessels and therefore help prevent the digression of the disease.^[20]

Pathology

Elevated levels of ACE are also found in sarcoidosis, and are used in diagnosing and monitoring this disease. Elevated levels of ACE are also found in leprosy, hyperthyroidism, acute hepatitis, primary biliary cirrhosis, diabetes mellitus, multiple myeloma, osteoarthritis, amyloidosis, Gaucher disease, pneumoconiosis, histoplasmosis, miliary tuberculosis.
Serum levels are decreased in renal disease, obstructive pulmonary disease, and hypothyroidism.

Influence on athletic performance

Studies have shown that different genotypes of angiotensin converting enzyme can lead to varying influence on athletic performance. ACE I/D polymorphism consists of either an insertion (I) or absence (D) of a 287 base pair alanine sequence in intron 16 of the gene.^[21] People carrying the I-allele usually have lower ACE levels while people carrying the D-allele have higher ACE levels.

People carrying the D-allele are associated with higher ACE levels that cause higher levels of angiotensin II. During physical exercise the blood pressure of D-allele carriers will therefore increase sooner than for I-allele carriers. This results in a lower maximal heart rate and lower maximum oxygen uptake (VO_2max). Therefore, D-allele carriers have a 10% increased risk of cardiovascular diseases. Furthermore, the D-allele is associated with a greater increase in left ventricular growth in response to training compared to the I-allele.^[22] On the other hand, I-allele carriers usually show an increased maximal heart rate due to lower ACE levels, higher maximum oxygen uptake and therefore show an enhanced endurance performance.^[22]

The I allele is found with increased frequency in elite distance runners, rowers and cyclists. Short distance swimmers show a higher occurrence of D-allele carriers in their specific discipline, since their discipline relies more on strength than endurance.^[23]^[24]

References

^ "Drugs that physically interact with Angiotensin I converting enzyme view/edit references on wikidata".
^ "Human PubMed Reference:".
^ "Mouse PubMed Reference:".
^ Skeggs LT, Kahn JR, Shumway NP (Mar 1956). "The preparation and function of the hypertensin-converting enzyme". The Journal of Experimental Medicine. 103 (3): 295–9. doi:10.1084/jem.103.3.295. PMC 2136590. PMID 13295487.
^ Kierszenbaum, Abraham L. (2007). Histology and cell biology: an introduction to pathology. Mosby Elsevier. ISBN 0-323-04527-8.
^ Fillardi P (2015). ACEi and ARBS in Hypertension and Heart Failure. Volume 5. Switzerland: Springer International Publishing. pp. 10–13. ISBN 978-3-319-09787-9.
^ Hemming ML, Selkoe DJ (Nov 2005). "Amyloid beta-protein is degraded by cellular angiotensin-converting enzyme (ACE) and elevated by an ACE inhibitor". The Journal of Biological Chemistry. 280 (45): 37644–50. doi:10.1074/jbc.M508460200. PMC 2409196. PMID 16154999.
^ ^a ^b Boulpaep EL, Boron WF (2005). "Integration of Salt and Water Balance". Medical Physiology: a Cellular and Molecular Approach. Philadelphia, Pa.: Elsevier Saunders. pp. 866–867. ISBN 978-1-4160-2328-9.
^ Coates D (Jun 2003). "The angiotensin converting enzyme (ACE)". The International Journal of Biochemistry & Cell Biology. Renin-Angiotensin Systems: State of the Art. 35 (6): 769–73. doi:10.1016/S1357-2725(02)00309-6. PMID 12676162.
^ Zhang R, Xu X, Chen T, Li L, Rao P (May 2000). "An assay for angiotensin-converting enzyme using capillary zone electrophoresis". Analytical Biochemistry. 280 (2): 286–90. doi:10.1006/abio.2000.4535. PMID 10790312.
^ Imig JD (Mar 2004). "ACE Inhibition and Bradykinin-Mediated Renal Vascular Responses: EDHF Involvement". Hypertension. 43 (3): 533–5. doi:10.1161/01.HYP.0000118054.86193.ce. PMID 14757781.
^ Wang W, McKinnie SM, Farhan M, Paul M, McDonald T, McLean B, Llorens-Cortes C, Hazra S, Murray AG, Vederas JC, Oudit GY (May 2016). "Angiotensin Converting Enzyme 2 Metabolizes and Partially Inactivates Pyrapelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System". Hypertension. 68: 365–77. doi:10.1161/HYPERTENSIONAHA.115.06892. PMID 27217402.
^ Bünning P, Riordan JF (Jul 1985). "The functional role of zinc in angiotensin converting enzyme: implications for the enzyme mechanism". Journal of Inorganic Biochemistry. 24 (3): 183–98. doi:10.1016/0162-0134(85)85002-9. PMID 2995578.
^ ^a ^b ^c Zhang C, Wu S, Xu D (Jun 2013). "Catalytic mechanism of angiotensin-converting enzyme and effects of the chloride ion". The Journal of Physical Chemistry B. 117 (22): 6635–45. doi:10.1021/jp400974n. PMID 23672666.
^ ^a ^b Bünning P (1983). "The catalytic mechanism of angiotensin converting enzyme". Clinical and Experimental Hypertension. Part A, Theory and Practice. 5 (7-8): 1263–75. doi:10.3109/10641968309048856. PMID 6315268.
^ "Angiotensin converting enzyme (ace) inhibitors" (PDF). British Hypertension Society.
^ Klabunde RE. "ACE-inhibitors". Cardiovascular Pharmacology Concepts. cvpharmacology.com. Retrieved 2009-03-26.
^ Brooks L (2004). "The Importance of Treating the Blood Pressure: ACE Inhibitors May Slow Alzheimer's Disease". Medscape. Medscape Cardiology.
^ Qiu WQ, Mwamburi M, Besser LM, Zhu H, Li H, Wallack M, Phillips L, Qiao L, Budson AE, Stern R, Kowall N (2013-01-01). "Angiotensin converting enzyme inhibitors and the reduced risk of Alzheimer's disease in the absence of apolipoprotein E4 allele". Journal of Alzheimer's Disease. 37 (2): 421–8. doi:10.3233/JAD-130716. PMC 3972060. PMID 23948883.
^ "ACE Enzyme May Enhance Immune Responses And Prevent Alzheimer's". Science 2.0. Retrieved 2016-03-01.
^ Wang P, Fedoruk MN, Rupert JL (2008). "Keeping pace with ACE: are ACE inhibitors and angiotensin II type 1 receptor antagonists potential doping agents?". Sports Medicine. 38 (12): 1065–79. doi:10.2165/00007256-200838120-00008. PMID 19026021.
^ ^a ^b Montgomery HE, Clarkson P, Dollery CM, Prasad K, Losi MA, Hemingway H, Statters D, Jubb M, Girvain M, Varnava A, World M, Deanfield J, Talmud P, McEwan JR, McKenna WJ, Humphries S (Aug 1997). "Association of angiotensin-converting enzyme gene I/D polymorphism with change in left ventricular mass in response to physical training". Circulation. 96 (3): 741–7. doi:10.1161/01.CIR.96.3.741. PMID 9264477.
^ Sanders J, Montgomery H, Woods D (2001). "Kardiale Anpassung an Körperliches Training" [The cardiac response to physical training] (PDF). Deutsche Zeitschrift für Sportmednizin (in German). pp. 86–92.
^ Costa AM, Silva AJ, Garrido ND, Louro H, de Oliveira RJ, Breitenfeld L (Aug 2009). "Association between ACE D allele and elite short distance swimming". European Journal of Applied Physiology. 106 (6): 785–90. doi:10.1007/s00421-009-1080-z. PMID 19458960.

External links

Proteopedia Angiotensin-converting_enzyme - the Angiotensin-Converting Enzyme Structure in Interactive 3D
Angiotensin Converting Enzyme at the US National Library of Medicine Medical Subject Headings (MeSH)
Human ACE genome location and ACE gene details page in the UCSC Genome Browser.

UpToDate Contents

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…into a pocket of the 23S subunit of the 50S ribosome specifically by attaching at domain V of the peptidyl transferase loop, thereby blocking protein assembly. In doing so, these drugs exert a bactericidal…
3. 研究用生物学的マーカーによる関節リウマチの診断および評価まinvestigational biologic markers in the diagnosis and assessment of rheumatoid arthritis [show details]
…SLE (2.7, 2.1, and 2.1 percent, respectively) . Antibodies to PADI4 – It is known that the enzyme peptidyl-arginine deiminase 4 (PADI4) converts arginine to citrulline and that genetic variants of this enzyme …
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English Journal

Angiotensin-(1-7) in kidney disease: a review of the controversies.

Zimmerman D, Burns KD.SourceKidney Research Centre, Division of Nephrology, Department of Medicine, Ottawa Hospital Research Institute, Ottawa, ON, Canada K1H 7W9.
Clinical science (London, England : 1979).Clin Sci (Lond).2012 Sep;123(6):333-46.
Ang-(1-7) [angiotensin-(1-7)] is a biologically active heptapeptide component of the RAS (renin-angiotensin system), and is generated in the kidney at relatively high levels, via enzymatic pathways that include ACE2 (angiotensin-converting enzyme 2). The biological effects of Ang-(1-7) in the kidney
PMID 22639821

Update on new aspects of the renin-angiotensin system in liver disease: clinical implications and new therapeutic options.

Grace JA, Herath CB, Mak KY, Burrell LM, Angus PW.SourceDepartment of Medicine, The University of Melbourne, Austin Hospital, Heidelberg, Melbourne, Victoria, Australia. j.grace4@pgrad.unimelb.edu.au
Clinical science (London, England : 1979).Clin Sci (Lond).2012 Aug 1;123(4):225-39.
The RAS (renin-angiotensin system) is now recognized as an important regulator of liver fibrosis and portal pressure. Liver injury stimulates the hepatic expression of components of the RAS, such as ACE (angiotensin-converting enzyme) and the AT(1) receptor [AngII (angiotensin II) type 1 receptor],
PMID 22548407

Japanese Journal

エンケファリン不活性化酵素

日本薬理学雑誌 101(4), 197-207, 1993
NAID 130000760221

Endopeptidase-24.11 is striosomally ordered in pig brain and in contrast to aminopeptidase N and peptidyl dipeptidase A ("angiotensin converting enzyme"), is a marker for a set of striatal efferent fibers.

Neuroscience 27, 799-817, 1988
NAID 30008325296

Estimation of relative importance of three enzymes in the inactivation of (Met5)-enkephalin and (Met5)-enkephalin-Arg6 in three isolated preparations by employing the inhibitor specific for each enzyme.

The Japanese Journal of Pharmacology 44(3), 241-247, 1987
NAID 130000831914

「angiotensin I-converting enzyme」

ACE
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	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, 5AMA
Identifiers
Aliases	ACE, angiotensin I converting enzyme, ACE1, CD143, DCP, DCP1, ICH, MVCD3, Angiotensin-converting enzyme
External IDs	OMIM: 106180 MGI: 87874 HomoloGene: 37351 GeneCards: ACE
Targeted by Drug
	captopril, cilazapril anhydrous, enalapril, imidapril, trandolapril, zofenopril
Gene ontology
Molecular function	• tripeptidyl-peptidase activity; • zinc ion binding; • exopeptidase activity; • endopeptidase activity; • metal ion binding; • mitogen-activated protein kinase binding; • bradykinin receptor binding; • peptidase activity; • protein binding; • drug binding; • carboxypeptidase activity; • chloride ion binding; • actin binding; • mitogen-activated protein kinase kinase binding; • hydrolase activity; • metallodipeptidase activity; • metallopeptidase activity; • peptidyl-dipeptidase activity;
Cellular component	• cytoplasm; • integral component of membrane; • endosome; • membrane; • lysosome; • extracellular exosome; • external side of plasma membrane; • extracellular region; • plasma membrane; • extracellular space;
Biological process	• regulation of renal output by angiotensin; • antigen processing and presentation of peptide antigen via MHC class I; • angiotensin catabolic process in blood; • beta-amyloid metabolic process; • angiotensin maturation; • blood vessel remodeling; • regulation of vasoconstriction; • hematopoietic stem cell differentiation; • regulation of angiotensin metabolic process; • regulation of smooth muscle cell migration; • mononuclear cell proliferation; • regulation of systemic arterial blood pressure by renin-angiotensin; • arachidonic acid secretion; • peptide catabolic process; • regulation of blood vessel diameter; • kidney development; • neutrophil mediated immunity; • proteolysis; • spermatogenesis; • regulation of blood pressure; • hormone catabolic process; • heart contraction; • positive regulation of protein tyrosine kinase activity; • cell proliferation in bone marrow; • positive regulation of peptidyl-tyrosine autophosphorylation; • regulation of hematopoietic stem cell proliferation; • negative regulation of gap junction assembly; • positive regulation of peptidyl-cysteine S-nitrosylation;
	Sources:Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	1636
	11421
	ENSG00000159640
	ENSMUSG00000020681
	P12821
	P09470
	NM_000789; NM_001178057; NM_152830; NM_152831
	NM_009598; NM_207624; NM_001281819
	NP_000780; NP_001171528; NP_690043
	NP_033728.1; NP_997507.1; NP_001268748; NP_033728; NP_997507
	Wikidata
View/Edit Human	View/Edit Mouse

Search
PMC	articles
PubMed	articles
NCBI	proteins

Angiotensin-converting enzyme
Identifiers
EC number	3.4.15.1
CAS number	9015-82-1
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search
PMC	articles
PubMed	articles
NCBI	proteins

　　[★]

アンジオテンシンI変換酵素、アンギオテンシンI変換酵素

関: angiotensin-converting enzyme、peptidyl-dipeptidase A

「ペプチジルジペプチダーゼA」

　　[★]

英: peptidyl-dipeptidase A
関: アンギオテンシン変換酵素、アンジオテンシンI変換酵素

「A」

　　[★]

「Ad」

　　[★]

アデノウイルス

関: adenoviral、adenovirus

「peptidyl dipeptidase」

　　[★] アンジオテンシン変換酵素

[1] "Drugs that physically interact with Angiotensin I converting enzyme view/edit references on wikidata".

[2] "Human PubMed Reference:".

[3] "Mouse PubMed Reference:".

[Skeggs_1956-4] Skeggs LT, Kahn JR, Shumway NP (Mar 1956). "The preparation and function of the hypertensin-converting enzyme". The Journal of Experimental Medicine. 103 (3): 295–9. doi:10.1084/jem.103.3.295. PMC 2136590. PMID 13295487.

[isbn0-323-04527-8-5] Kierszenbaum, Abraham L. (2007). Histology and cell biology: an introduction to pathology. Mosby Elsevier. ISBN 0-323-04527-8.

[6] Fillardi P (2015). ACEi and ARBS in Hypertension and Heart Failure. Volume 5. Switzerland: Springer International Publishing. pp. 10–13. ISBN 978-3-319-09787-9.

[Hemming_2005-7] Hemming ML, Selkoe DJ (Nov 2005). "Amyloid beta-protein is degraded by cellular angiotensin-converting enzyme (ACE) and elevated by an ACE inhibitor". The Journal of Biological Chemistry. 280 (45): 37644–50. doi:10.1074/jbc.M508460200. PMC 2409196. PMID 16154999.

[Boron_2005-8] Boulpaep EL, Boron WF (2005). "Integration of Salt and Water Balance". Medical Physiology: a Cellular and Molecular Approach. Philadelphia, Pa.: Elsevier Saunders. pp. 866–867. ISBN 978-1-4160-2328-9.

[9] Coates D (Jun 2003). "The angiotensin converting enzyme (ACE)". The International Journal of Biochemistry & Cell Biology. Renin-Angiotensin Systems: State of the Art. 35 (6): 769–73. doi:10.1016/S1357-2725(02)00309-6. PMID 12676162.

[pmid10790312-10] Zhang R, Xu X, Chen T, Li L, Rao P (May 2000). "An assay for angiotensin-converting enzyme using capillary zone electrophoresis". Analytical Biochemistry. 280 (2): 286–90. doi:10.1006/abio.2000.4535. PMID 10790312.

[pmid14757781-11] Imig JD (Mar 2004). "ACE Inhibition and Bradykinin-Mediated Renal Vascular Responses: EDHF Involvement". Hypertension. 43 (3): 533–5. doi:10.1161/01.HYP.0000118054.86193.ce. PMID 14757781.

[12] Wang W, McKinnie SM, Farhan M, Paul M, McDonald T, McLean B, Llorens-Cortes C, Hazra S, Murray AG, Vederas JC, Oudit GY (May 2016). "Angiotensin Converting Enzyme 2 Metabolizes and Partially Inactivates Pyrapelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System". Hypertension. 68: 365–77. doi:10.1161/HYPERTENSIONAHA.115.06892. PMID 27217402.

[13] Bünning P, Riordan JF (Jul 1985). "The functional role of zinc in angiotensin converting enzyme: implications for the enzyme mechanism". Journal of Inorganic Biochemistry. 24 (3): 183–98. doi:10.1016/0162-0134(85)85002-9. PMID 2995578.

[Zhang_2013-14] Zhang C, Wu S, Xu D (Jun 2013). "Catalytic mechanism of angiotensin-converting enzyme and effects of the chloride ion". The Journal of Physical Chemistry B. 117 (22): 6635–45. doi:10.1021/jp400974n. PMID 23672666.

[B.C3.BCnning_1983-15] Bünning P (1983). "The catalytic mechanism of angiotensin converting enzyme". Clinical and Experimental Hypertension. Part A, Theory and Practice. 5 (7-8): 1263–75. doi:10.3109/10641968309048856. PMID 6315268.

[16] "Angiotensin converting enzyme (ace) inhibitors" (PDF). British Hypertension Society.

[urlACE-inhibitors-17] Klabunde RE. "ACE-inhibitors". Cardiovascular Pharmacology Concepts. cvpharmacology.com. Retrieved 2009-03-26.

[18] Brooks L (2004). "The Importance of Treating the Blood Pressure: ACE Inhibitors May Slow Alzheimer's Disease". Medscape. Medscape Cardiology.

[19] Qiu WQ, Mwamburi M, Besser LM, Zhu H, Li H, Wallack M, Phillips L, Qiao L, Budson AE, Stern R, Kowall N (2013-01-01). "Angiotensin converting enzyme inhibitors and the reduced risk of Alzheimer's disease in the absence of apolipoprotein E4 allele". Journal of Alzheimer's Disease. 37 (2): 421–8. doi:10.3233/JAD-130716. PMC 3972060. PMID 23948883.

[20] "ACE Enzyme May Enhance Immune Responses And Prevent Alzheimer's". Science 2.0. Retrieved 2016-03-01.

[pmid19026021-21] Wang P, Fedoruk MN, Rupert JL (2008). "Keeping pace with ACE: are ACE inhibitors and angiotensin II type 1 receptor antagonists potential doping agents?". Sports Medicine. 38 (12): 1065–79. doi:10.2165/00007256-200838120-00008. PMID 19026021.

[Montgomery_1997-22] Montgomery HE, Clarkson P, Dollery CM, Prasad K, Losi MA, Hemingway H, Statters D, Jubb M, Girvain M, Varnava A, World M, Deanfield J, Talmud P, McEwan JR, McKenna WJ, Humphries S (Aug 1997). "Association of angiotensin-converting enzyme gene I/D polymorphism with change in left ventricular mass in response to physical training". Circulation. 96 (3): 741–7. doi:10.1161/01.CIR.96.3.741. PMID 9264477.

[23] Sanders J, Montgomery H, Woods D (2001). "Kardiale Anpassung an Körperliches Training" [The cardiac response to physical training] (PDF). Deutsche Zeitschrift für Sportmednizin (in German). pp. 86–92.

[pmid19458960-24] Costa AM, Silva AJ, Garrido ND, Louro H, de Oliveira RJ, Breitenfeld L (Aug 2009). "Association between ACE D allele and elite short distance swimming". European Journal of Applied Physiology. 106 (6): 785–90. doi:10.1007/s00421-009-1080-z. PMID 19458960.

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)

1-50	CD1 a-c 1A 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50

51-100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100

101-150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150

151-200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200

201-250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249

251-300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299

301-350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

v t e Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

リンク元	「angiotensin I-converting enzyme」「ペプチジルジペプチダーゼA」
関連記事	「A」「Ad」「peptidyl dipeptidase」

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peptidyl-dipeptidase A