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

WordNet

the 9th letter of the Roman alphabet (同)i
any of several complex proteins that are produced by cells and act as catalysts in specific biochemical reactions
any of several vasoconstrictor substances (trade name Hypertensin) that cause narrowing of blood vessels (同)angiotonin, Hypertensin

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『私は』私が
iodineの化学記号
酵素

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/08/14 18:29:18」(JST)

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Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure.

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.

ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels.^[1]

Functions

Schematic diagram of the renin–angiotensin–aldosterone system

Anatomical diagram of the renin-angiotensin system, showing the role of ACE at the lungs.^[2]

It has two primary functions:

ACE catalyses the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor in a substrate concentration-dependent manner.^[3]
ACE degrades bradykinin, a potent vasodilator, and other vasoactive peptides,^[4]

These two actions make ACE inhibition a goal in the treatment of conditions such as high blood pressure, heart failure, diabetic nephropathy, and type 2 diabetes mellitus. Inhibition of ACE (by ACE inhibitors) results in the decreased formation of angiotensin II and decreased metabolism of bradykinin, leading 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.^[5]

Genetics and C and N domains function

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 RAAS 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 select N terminal activity may, therefore, cause accumulation of Aβ42 and progression of dementia.^{[citation needed]}

Pathology

Elevated levels of ACE are 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

ACE gene is a I/D polymorphism leading to the presence(I) or absence (D) the carriers of the ACE insertion allele of an alu repeat in intron 16 of the gene.^[6] With the insertion, observed higher maximum oxygen uptake (VO2max), increase in training, and increased muscle when paired with individuals carrying the deletion allele.
Individuals with the insertion are associated with long distance and endurance events. This is seen in studies that suggest that it is due to lower levels of angiotensin II. The deletion of the Alu increases angiotensin II that in turn increases the vasoconstriction of blood vessels. This is observed in short distance events and seen mostly in swimmers.^[7]

References

^ Kierszenbaum, Abraham L. (2007). Histology and cell biology: an introduction to pathology. Mosby Elsevier. ISBN 0-323-04527-8.
^ Page 866-867 (Integration of Salt and Water Balance) and 1059 (The Adrenal Gland) in: Walter F., PhD. Boron (2003). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. p. 1300. ISBN 1-4160-2328-3.
^ Zhang R, Xu X, Chen T, Li L, Rao P (May 2000). "An assay for angiotensin-converting enzyme using capillary zone electrophoresis". Anal. Biochem. 280 (2): 286–90. doi:10.1006/abio.2000.4535. PMID 10790312.
^ Imig JD (March 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.
^ Klabunde RE. "ACE-inhibitors". Cardiovascular Pharmacology Concepts. cvpharmacology.com. Retrieved 2009-03-26.
^ 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 Med 38 (12): 1065–79. doi:10.2165/00007256-200838120-00008. PMID 19026021.
^ Costa AM, Silva AJ, Garrido ND, Louro H, de Oliveira RJ, Breitenfeld L (August 2009). "Association between ACE D allele and elite short distance swimming". Eur. J. Appl. Physiol. 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)

UpToDate Contents

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1. 肺サルコイドーシスの臨床症状および診断 clinical manifestations and diagnosis of pulmonary sarcoidosis
2. Overview of the renin-angiotensin system
3. 心不全におけるアンギオテンシン変換酵素阻害剤およびアンギオテンシン受容体拮抗剤：作用機序 angiotensin converting enzyme inhibitors and receptor blockers in heart failure mechanisms of action
4. アンギオテンシン変換酵素阻害剤とアンギオテンシン受容体拮抗剤との相違 differences between angiotensin converting enzyme inhibitors and receptor blockers
5. 急性心筋梗塞におけるアンギオテンシン変換酵素阻害剤：作用機序 angiotensin converting enzyme inhibitors in acute myocardial infarction mechanisms of action

English Journal

Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC-MS/MS.

Lau CC, Abdullah N, Shuib AS, Aminudin N.Author information Mushroom Research Centre, Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia.AbstractAngiotensin I-converting enzyme (ACE) inhibitors derived from foods are valuable auxiliaries to agents such as captopril. Eight highly functional ACE inhibitory peptides from the mushroom, Agaricus bisporus, were identified by LC-MS/MS. Among these peptides, the most potent ACE inhibitory activity was exhibited by AHEPVK, RIGLF and PSSNK with IC₅₀ values of 63, 116 and 129 μM, respectively. These peptides exhibited high ACE inhibitory activity after gastrointestinal digestion. Lineweaver-Burk plots suggested that AHEPVK and RIGLF act as competitive inhibitors against ACE, whereas PSSNK acts as a non-competitive inhibitor. Mushrooms can be a good component of dietary supplement due to their readily available source and, in addition, they rarely cause food allergy. Compared to ACE inhibitory peptides isolated from other edible mushrooms, AHEPVK, RIGLF and PSSNK have lower IC₅₀ values. Therefore, these peptides may serve as an ideal ingredient in the production of antihypertensive supplements.
Food chemistry.Food Chem.2014 Apr 1;148:396-401. doi: 10.1016/j.foodchem.2013.10.053. Epub 2013 Oct 24.
Angiotensin I-converting enzyme (ACE) inhibitors derived from foods are valuable auxiliaries to agents such as captopril. Eight highly functional ACE inhibitory peptides from the mushroom, Agaricus bisporus, were identified by LC-MS/MS. Among these peptides, the most potent ACE inhibitory activity w
PMID 24262574

Application of taste sensing system for characterisation of enzymatic hydrolysates from shrimp processing by-products.

Cheung IW, Li-Chan EC.Author information The University of British Columbia, Faculty of Land and Food Systems, Food Nutrition and Health Program, 2205 East Mall, Vancouver, British Columbia V6T 1Z4, Canada.AbstractThe objective of this study was to investigate the potential of an instrumental taste-sensing system to distinguish between shrimp processing by-products hydrolysates produced using different proteases and hydrolysis conditions, and the possible association of taste sensor outputs with human gustatory assessment, salt content, and bioactivity. Principal component analysis of taste sensor output data categorised samples according to the proteases used for hydrolysis. High umami sensor outputs were characteristic of bromelain- and Flavourzyme-produced hydrolysates, compared to low saltiness and high bitterness outputs of Alcalase-produced hydrolysates, and high saltiness and low umami outputs of Protamex-produced hydrolysates. Extensively hydrolysed samples showed higher sourness outputs. Saltiness sensor outputs were correlated with conductivity and sodium content, while umami sensor responses were related to gustatory sweetness, bitterness and umami, as well as angiotensin-I converting enzyme inhibitory activity. Further research should explore the dose dependence and sensitivity of each taste sensor to specific amino acids and peptides.
Food chemistry.Food Chem.2014 Feb 15;145:1076-85. doi: 10.1016/j.foodchem.2013.09.004. Epub 2013 Sep 11.
The objective of this study was to investigate the potential of an instrumental taste-sensing system to distinguish between shrimp processing by-products hydrolysates produced using different proteases and hydrolysis conditions, and the possible association of taste sensor outputs with human gustato
PMID 24128587

Fragment-based design for the development of N-domain-selective angiotensin-1-converting enzyme inhibitors.

Douglas RG, Sharma RK, Masuyer G, Lubbe L, Zamora I, Acharya KR, Chibale K, Sturrock ED.Author information *Institute of Infectious Disease and Molecular Medicine, and Division of Medical Biochemistry, University of Cape Town, Observatory, Cape Town 7935, South Africa.AbstractACE (angiotensin-1-converting enzyme) is a zinc metallopeptidase that plays a prominent role in blood pressure regulation and electrolyte homeostasis. ACE consists of two homologous domains that despite similarities of sequence and topology display differences in substrate processing and inhibitor binding. The design of inhibitors that selectively inhibit the N-domain (N-selective) could be useful in treating conditions of tissue injury and fibrosis due to build-up of N-domain-specific substrate Ac-SDKP (N-acetyl-Ser-Asp-Lys-Pro). Using a receptor-based SHOP (scaffold hopping) approach with N-selective inhibitor RXP407, a shortlist of scaffolds that consisted of modified RXP407 backbones with novel chemotypes was generated. These scaffolds were selected on the basis of enhanced predicted interaction energies with N-domain residues that differed from their C-domain counterparts. One scaffold was synthesized and inhibitory binding tested using a fluorogenic ACE assay. A molecule incorporating a tetrazole moiety in the P2 position (compound 33RE) displayed potent inhibition (K(i)=11.21±0.74 nM) and was 927-fold more selective for the N-domain than the C-domain. A crystal structure of compound 33RE in complex with the N-domain revealed its mode of binding through aromatic stacking with His388 and a direct hydrogen bond with the hydroxy group of the N-domain specific Tyr369. This work further elucidates the molecular basis for N-domain-selective inhibition and assists in the design of novel N-selective ACE inhibitors that could be employed in treatment of fibrosis disorders.
Clinical science (London, England : 1979).Clin Sci (Lond).2014 Feb;126(4):305-13. doi: 10.1042/CS20130403.
ACE (angiotensin-1-converting enzyme) is a zinc metallopeptidase that plays a prominent role in blood pressure regulation and electrolyte homeostasis. ACE consists of two homologous domains that despite similarities of sequence and topology display differences in substrate processing and inhibitor b
PMID 24015848

Japanese Journal

Essential Oil Composition, Antioxidant, Antidiabetic and Antihypertensive Properties of Two <i>Afromomum</i> Species

Journal of Oleo Science 66(1), 51-63, 2017
NAID 130005180985

アンジオテンシン変換酵素阻害ペプチド高含有醤油の血圧降下作用

日本醸造協会誌 111(5), 302-307, 2016-05
NAID 40020864791

Angiotensin Ⅰ-Converting Enzyme and Lipase Inhibitory Activities of Kabosu Juice (Citrus sphaerocarpa Hort. ex Tanaka)

中村学園大学・中村学園大学短期大学部研究紀要 (48), 181-185, 2016-03
NAID 120005850761

「アンジオテンシンI変換酵素」

Angiotensin I converting enzyme
	Rendering of ACE from PDB 1O86
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, 3L3N, 3NXQ, 4APH, 4APJ, 4BXK, 4BZR, 4BZS, 4C2N, 4C2O, 4C2P, 4C2Q, 4C2R, 4CA5, 4CA6
Identifiers
Symbols	ACE ; ACE1; CD143; DCP; DCP1; ICH; MVCD3
External IDs	OMIM: 106180 MGI: 87874 HomoloGene: 37351 ChEMBL: 1808 GeneCards: ACE Gene
EC number	3.4.15.1
Gene ontology
Molecular function	• actin binding; • endopeptidase activity; • carboxypeptidase activity; • protein binding; • drug binding; • metallopeptidase activity; • exopeptidase activity; • tripeptidyl-peptidase activity; • peptidyl-dipeptidase activity; • zinc ion binding; • chloride ion binding; • mitogen-activated protein kinase kinase binding; • bradykinin receptor binding; • mitogen-activated protein kinase binding;
Cellular component	• extracellular region; • extracellular space; • lysosome; • endosome; • plasma membrane; • external side of plasma membrane; • integral component of membrane; • extracellular exosome;
Biological process	• kidney development; • blood vessel remodeling; • angiotensin maturation; • angiotensin catabolic process in blood; • regulation of renal output by angiotensin; • neutrophil mediated immunity; • antigen processing and presentation of peptide antigen via MHC class I; • regulation of systemic arterial blood pressure by renin-angiotensin; • spermatogenesis; • regulation of blood pressure; • regulation of smooth muscle cell migration; • regulation of vasoconstriction; • mononuclear cell proliferation; • regulation of vasodilation; • hormone catabolic process; • peptide catabolic process; • cellular protein metabolic process; • beta-amyloid metabolic process; • arachidonic acid secretion; • heart contraction; • regulation of angiotensin metabolic process; • hematopoietic stem cell differentiation; • 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
	v; t; e;

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
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PMC	articles
PubMed	articles
NCBI	proteins

　　[★]

英: angiotensin I-converting enzyme
関: アンギオテンシン変換酵素、アンギオテンシンI変換酵素、ペプチジルジペプチダーゼA

「peptidyl-dipeptidase A」

　　[★]

ペプチジルジペプチダーゼA

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

「アンギオテンシンI変換酵素」

　　[★]

英: angiotensin I-converting enzyme
関: アンジオテンシンI変換酵素

「I」

　　[★]

「Id」

　　[★]

イディオタイプ idiotype idiotypic
inhibitor of DNA binding

「angiotensin」

　　[★] アンジオテンシン

[isbn0-323-04527-8-1] Kierszenbaum, Abraham L. (2007). Histology and cell biology: an introduction to pathology. Mosby Elsevier. ISBN 0-323-04527-8.

[2] Page 866-867 (Integration of Salt and Water Balance) and 1059 (The Adrenal Gland) in: Walter F., PhD. Boron (2003). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. p. 1300. ISBN 1-4160-2328-3.

[pmid10790312-3] Zhang R, Xu X, Chen T, Li L, Rao P (May 2000). "An assay for angiotensin-converting enzyme using capillary zone electrophoresis". Anal. Biochem. 280 (2): 286–90. doi:10.1006/abio.2000.4535. PMID 10790312.

[pmid14757781-4] Imig JD (March 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.

[urlACE-inhibitors-5] Klabunde RE. "ACE-inhibitors". Cardiovascular Pharmacology Concepts. cvpharmacology.com. Retrieved 2009-03-26.

[pmid19026021-6] 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 Med 38 (12): 1065–79. doi:10.2165/00007256-200838120-00008. PMID 19026021.

[pmid19458960-7] Costa AM, Silva AJ, Garrido ND, Louro H, de Oliveira RJ, Breitenfeld L (August 2009). "Association between ACE D allele and elite short distance swimming". Eur. J. Appl. Physiol. 106 (6): 785–90. doi:10.1007/s00421-009-1080-z. PMID 19458960.

リンク元	「アンジオテンシンI変換酵素」「peptidyl-dipeptidase A」「アンギオテンシンI変換酵素」
関連記事	「I」「Id」「angiotensin」

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案内

angiotensin I-converting enzyme