Angiotensin-I converting Enzyme

Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, Tregear et al. Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci USA 1988 85 9386-9390. 

WlNKELMANN BR, NAUCK M, KlEIN B, Russ AP, Bohm BO, Siekmeier R, Ihn-ken K, Verho M, Gross W, Marz W. Deletion polymorphism of the angiotensin I-converting enzyme gene Is associated with increased plasma angiotensin-con-verting enzyme activity but not with increased risk for myocardial infarction and coronary artery disease. Ann Intern Med 1996 125 19-25. 

Membrane alanyl aminopeptidase (microsomal aminopeptidase, amino-peptidase M, EC 3.4.11.2) and peptidyl-dipeptidase A (angiotensin I converting enzyme, EC 3.4.15.1) located in the vascular endothelium and smooth muscle cell surface modulate the levels of vasoactive peptides [23], One of the roles of membrane-bound enzymes is to switch off the action of peptides in the vicinity of the target or to prevent them from gaining access to a region containing receptors that are activated only by locally released peptides. 

Peptidyl-dipeptidase A (angiotensin-I converting enzyme, ACE, EC 3.4.15.1) plays a pivotal role in the control of blood pressure [80]. It has been established that its active site contains an essential Zn-atom that functions like that of carboxypeptidase A [2], ACE is inhibited by peptides having a proline or aromatic amino acid at the C-terminal position. These observations as well as the similarities with the active site of carboxypeptidase A have allowed a rational design of effective inhibitors of ACE (e.g., captopril (3.4) and enalapril (3.5)) used in the treatment of hypertension [81]. 

Skidgel, R.A., Erdos, E.G. (1985) Novel activity of human angiotensin I converting enzyme release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone. Proc. Natl. Acad. Sci. U. S. A., 82, 1025-1029. 

Scacchi, R., De Bernardini, L., Mantuano, E., et al. (1998) DNA polymorphisms of apoUpo-protein B and angiotensin I-converting enzyme genes and relationships with Upid levels in Italian patients with vascular dementia or Alzheimer s disease. Dement. Geriatr. Cogn. Disord., 9, 186-190. 

Wu, C., Zhou, D., Guan, Z., Fan, J., Qio, Y. (2002) The association between angiotensin I converting enzyme gene polymorphism and Chinese late onset Alzheimer disease. Zhonghua Yi Xue Yi Chuan Xue Za Zhi, 19, 401-404. 

Matsui T, Ueno T, Tanaka M, Oka H, Miyamoto T, Osajima K, Matsumoto K. (2005) Antiproliferation action of an angiotensin I-converting enzyme inhibitory peptide, Val-Tyr, via an L-type Ca channel inhibition in cultured vascular smooth muscle cells. Hypertens Res 28 545-552. 

Arihara K, Nakashima Y, Mukai T, Ishikawa S, Itoh M. (2001) Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins. Meat Sci 57 319-324. 

Hyoung LD, Ho KJ, Sik PJ, Jun CY, Soo LJ. (2004) Isolation and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from the edible mushroom Tricholoma giganteum. Peptides 25 621-627. 

Vercruysse L, Smagghe G, Matsui T, Camp JV. (2008) Purification and identification of an angiotensin I-converting enzyme (ACE) inhibitory peptide from the gastrointestinal hydrolysate of the cotton leafworm, Spodoptera Littoralis. Process Biochem 43 900-904. 

Matsui T, Yoo HI, Hwang IS, Lee DS, Kim HB. (2004) Isolation of angiotensin I-converting enzyme inhibitory peptide from Chungkookjang. Korean J Microbiol 40 355-358. 

Kuba M, Tanaka K, Tawata S, Takeda Y, Yasuda M. (2003) Angiotensin I-converting enzyme inhibitory peptides isolated from tofuyo fermented soybean food. Biosci Biotechnol Biochem 67 1278-1283. 

Suetsuna K. (1998) Isolation and characterization of angiotensin I-converting enzyme inhibitor dipeptides derived from Allium sativum L (garlic). J Nutr Biochem 9 415—419. 

Inhibitors of the angiotensin I-converting enzyme (ACE-inhibitors) have been introduced into cardiovascular medicine, in particular for the treatment of hypertension and congestive heart failure (CHE). 

Hamamoto, H., Sugiyama, Y, and Nakagawa, N. et al. (1993). A new tobacco mosaic vims vector and its use for the systemic production of angiotensin-I-converting enzyme inhibitor in transgenic tobacco and tomato. Bio/ Technology 11 930-932. 

Mollusks along with the crustaceans are also widely sought to participate in the world s consumption of marine food. Fermented marine food sauces such as blue mussel sauce and oyster sauce possess bioactive peptides which play a major role as Angiotensin I converting enzyme inhibitors that indirectly suppress hypertension (Wijesekara and Kim, 2010). Hence, the mollusk-derived proteins and other macromolecules are highly valuable to indicate these organisms as medicinally valuable food sources. 

Wijesekara, I. and Kim, S. K. (2010). Angiotensin-i-converting enzyme (ace) inhibitors from marine resources Prospects in the pharmaceutical industry. Mar. Drugs 8,1080-1093. 

Byun, H. G. and Kim, S. K. (2001). Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska Pollack (Theragra chalcogramma) skin. Process Biochem. 36,1155-1162. 

Cheung, I. W. Y. and Li-Chan, E. C. Y. (2010). Angiotensin-I-converting enzyme inhibitory activity and bitterness of enzymatically-produced hydrolysates of shrimp (Pandalopsis dispar) processing byproducts investigated by Taguchi design. Food Chem. 122,1003-1012. 

Fahmi, A., Morimura, S., Gou, H. C., Shinematsu, T., Kida, K., and Uemura, Y. (2004). Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales. Process Biochem. 39,1195-1200. 

He, H. L., Chen, X. L., Sun, S. Y., Zhang, Y. Z., and Zhou, . C. (2006). Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis. ]. Pept. Sci. 12, 726-733. 

Katano, S., Oki, T., Matsuo, Y., Yoshihira, K., Nara, Y., Miki, T., Matsui, T., and Matsumoto, K. (2003). Antihypertensive effect of alkaline protease hydrolysate of the pearl oyster Pinctada fucata martencii separation and identification of angiotensin-I converting enzyme inhibitory peptides. Nippon Suisan Gakk. 69, 975-980. 

Lee, J. K., Jeon, J. K., and Byun, H. G. (2011). Effect of angiotensin I converting enzyme inhibitory peptide purified from skate skin hydrolysate. Food Chem. 125, 495-499. 

Matsufuji, H., Matsui, T., Seki, E., Osajima, K., Nakashima, M., and Osajima, Y. (1994). Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle. Biosci. Biotechnol. Biochem. 58, 2244-2245. 

Shiozaki, K., Shiozaki, M., Masuda, J., Yamauchi, A., Ohwada, S., Nakano, T., Yamaguchi, T., Saito, T., Muranoto, K., and Sato, M. (2010). Identification of oyster-derived hypotensive peptide acting as angiotensin-I-converting enzyme inhibitor. Fish Sci. 76, 865-872. 

Tsai, J. S., Lin, T. C, Chen, J. L., and Pan, B. S. (2006). The inhibitory effects of freshwater clam (Corbicula fluminea, Muller) muscle protein hydrolysate on angiotensin I converting enzyme. Process Biochem. 41, 2276-2281. 

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