Differences in the hydrolysis of enkephalin congeners by the two domains of angiotensin converting enzyme

Biochemical Pharmacology

Volumn 53, Issue 10, 1997, Pages 1459-1463

  Deddish, Peter A ^a   Jackman, Herbert L ^a   Skidgel, Randal A ^a   Erdös, Ervin G ^a,b  

^a UNIVERSITY OF ILLINOIS   (United States)

^b UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

ACE C domain; ACE N domain; Chloride; Kininase II; Opioid peptides; Peptidyl dipeptidase

Indexed keywords

ALANINE; ARGININE; CHLORIDE ION; DIPEPTIDYL CARBOXYPEPTIDASE; ENKEPHALIN; GLYCINE; LEUCINE ENKEPHALIN; METENKEPHALIN; METENKEPHALIN[6 ARGININE 7 PHENYLALANINE]; OPIATE PEPTIDE; PHENYLALANINE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DRUG HYDROLYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; PRIORITY JOURNAL; PROTEIN DOMAIN;

EID: 0030790474     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(97)00087-7     Document Type: Article

References (33)

1. Soubrier F, Alhenc-Gelas F, Hubert C, Allegrini J, John M, Gregear G and Corvol P, Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci USA 85: 9386-9390, 1988.
2. Soubrier F, Wei L, Hubert C, Clauser E, Alhenc-Gelas F and Corvol P, Molecular biology of the angiotensin I converting enzyme: II. Structure-function. Gene polymorphism and clinical implications. J Hypertens 11: 599-604, 1993.
3. Soubrier F, Hubert C, Testut P, Nadaud S, Alhenc-Gelas F and Corvol P, Molecular biology of the angiotensin I converting enzyme: I. Biochemistry and structure of the gene. J Hypertens 11: 471-476, 1993.
4. Bernstein KE, Martin BM, Edwards AS and Bernstein EA, Mouse angiotensin-converting enzyme is a protein composed of two homologous domains. J Biol Chem 264: 11945-11951, 1989.
5. Skeggs LT Jr, Marsh WH, Kahn JR and Shumway NP, The purification of hypertensin I. J Exp Med 100: 363-370, 1954.
6. Igić R, Nakajima T, Yeh HSJ, Sorrells K and Erdös EG, Kininases. In: Pharmacology and the Future of Man - Proceedings of the 5th International Congress of Pharmacology (Ed. Acheson G), pp. 307-319. Karger, Basel, 1973.
7. Skidgel RA and Erdös EG, Biochemistry of angiotensin converting enzyme. In: The Renin Angiotensin System (Eds. Robertson JIS and Nicholls MG), Vol. 1, pp. 10.1-10.10. Gower Medical Publishers, London, 1993.
8. Ehlers MRW, Fox EA, Strydom DJ and Riordan JF, Molecular cloning of human testicular angiotensin-converting enzyme: The testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc Natl Acad Sci USA 86: 7741-7745, 1989.
9. Lattion A-L, Soubrier F, Allegrini J, Hubert C, Corvol P and Alhenc-Gelas F, The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme. FEBS Lett 252: 99-104, 1989.
10. Kumar RS, Kusari J, Roy SN, Soffer RL and Sen GC, Structure of testicular angiotensin-converting enzyme. A segmental mosaic enzyme. J Biol Chem 264: 16754-16758, 1989.
11. Kumar RS, Thekkumkara TJ and Sen GC, The mRNAs encoding the two angiotensin converting isozymes are transcribed from the same gene by a tissue-specific choice of alternative transcription initiation sites. J Biol Chem 266: 3854-3862, 1991.
12. Ehlers MRW and Riordan JF, Angiotensin-converting enzyme. Biochemistry and molecular biology. In: Hypertension: Pathophysiology, Diagnosis, and Management (Eds. Laragh JH and Brenner BM), 2nd Edn, pp. 1217-1231. Raven Press, New York, 1990.
13. Deddish PA, Wang J, Michel B, Morris PW, Davidson NO, Skidgel RA and Erdös EG, Naturally occurring active N-domain of human angiotensin I converting enzyme. Proc Natl Acad Sci USA 91: 7807-7811, 1994.
14. Deddish PA, Wang L-X, Jackman HL, Michel B, Wang J, Skidgel RA and Erdös EG, Single-domain angiotensin I converting enzyme (kininase II; ACE): Characterization and properties. J Pharmacol Exp Ther 279: 1582-1589, 1996.
15. Jaspard E, Wei L and Alhenc-Gelas F, Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides. J Biol Chem 268: 9496-9503, 1993.
16. Skidgel RA, Defendini R and Erdös EG, Angiotensin I converting enzyme and its role in neuropeptide metabolism. In: Neuropeptides and Their Peptidases (Ed. Turner AJ), pp. 165-182. Ellis-Horwood, Chichester, England, 1987.
17. Skidgel RA, Engelbrecht S, Johnson AR and Erdös EG, Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase. Peptides 5: 769-776, 1984.
18. 2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone. Proc Natl Acad Sci USA 82: 1025-1029, 1985.
19. Stewart TA, Weare JA and Erdös EG, Purification and characterization of human converting enzyme (kininase II). Peptides 2: 145-152, 1981.
20. Schwartz J-C, Metabolism of enkephalins and the inactivating neuropeptidase concept. Trends Neurosci 6: 15-18, 1983.
21. Erdös EG, Johnson AR and Boyden NT, Hydrolysis of enkephalin by cultured human endothelial cells and by purified peptidyl dipeptidase. Biochem Pharmacol 27: 843-848, 1978.
22. 7. Proc Natl Acad Sci USA 77: 5512-5514, 1980.
23. Lazarus LH, Bryant SD, Salvadori S, Attila M and Jones LS, Opioid infidelity: Novel opioid peptides with dual high affinity for δ and μ receptors. Trends Neurosci 19: 31-35, 1996.
24. 7 metabolism: Conversion to Met-enkephalin by brain and kidney dipeptidyl carboxypeptidases. Biochem Biophys Res Commun 99: 630-636, 1981.
25. 5]-enkephalin by dipeptidyl carboxypeptidase. Neuropharmacology 20: 891-894, 1981.
26. Bradford MM, A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72: 248-254, 1976.
27. Jackman HL, Tan F, Tamei H, Beurling-Harbury C, Li X-Y, Skidgel RA and Erdös EG, A peptidase in human platelets that deamidates tachykinins: Probable identity with the lysosomal "protective protein." J Biol Chem 265: 11265-11272, 1990.
28. Erspamer V, The opioid peptides of the amphibian skin. Int J Dev Neurosci 10: 3-30, 1992.
29. Wei L, Alhenc-Gelas F, Corvol P and Clauser E, The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J Biol Chem 266: 9002-9008, 1991.
30. Erdös EG and Skidgel RA, Human angiotensin I converting enzyme: Unusual substrate specificity and distribution. Hypertension 8 [Suppl I], 1-34-1-37, 1986.
31. Oshima G, Gecse A and Erdös EG, Angiotensin I converting enzyme of the kidney cortex. Biochim Biophys Acta 350: 26-37, 1974.
32. Rousseau A, Michaud A, Chauvet M-T, Lenfant M and Corvol P, The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme. J Biol Chem 270: 3656-3661, 1995.
33. 7 by inhibiting its degradation in mouse brain. Mol Pharmocol 28: 521-526, 1985.