Skeggs LT, Kahn JR, Shumway NP: Preparation and function of the hypertensin converting enzyme. J Exp Med. 1956, 103: 295-299. The first report on the isolation and partial characterization of ACE, in this case from horse plasma.
Hubert C, Houot AM, Corvol P, Soubrier F: Structure of the angiotensin I-converting enzyme gene. Two alternate promoters correspond to evolutionary steps of a duplicated gene. J Biol Chem. 1991, 266: 15377-15383. The complete description of the gene structure of sACE and evidence for alternative promoters for the expression of the mRNAs for somatic and germinal ACE.
Corvol P, Williams TA: Peptidyl-dipeptidase A/angiotensin 1-converting enzyme. In Handbook of Proteolytic Enzymes. Edited by: Barrett AJ, Rawlings ND, Woessner JF. 1998, San Diego: Academic Press, 1066-1076. An excellent summary of ACE, including sequence data bank codes and a thorough analysis of the chemical and biological properties of ACE.
Williams TA, Michaud A, Houard X, Chauvet M-T, Soubrier F, Corvol P: Drosophila melanogaster angiotensin I-converting enzyme expressed in Pichia pastoris resembles the C domain of the mammalian homologue and does not require glycosylation for secretion and enzymatic activity. Biochem J. 1996, 318: 125-131. This paper shows that AnCE has catalytic properties that resemble those of human C-domain ACE.
Cornell MJ, Williams TA, Lamango NS, Coates D, Corvol P, Soubrier F, Hoheisel J, Lehrach H, Isaac RE: Cloning and expression of an evolutionary conserved single-domain angiotensin converting enzyme from Drosophila melanogaster. J Biol Chem. 1995, 270: 13613-13619. 10.1074/jbc.270.29.17627. This paper presents an interesting analysis of the evolution of the ACE gene and its duplication.
Coates D, Isaac RE, Cotton J, Siviter R, Williams TA, Shirras A, Corvol P, Dive V: Functional conservation of the active sites of human and Drosophila angiotensin I-converting enzyme. Biochemistry. 2000, 39: 8963-8969. 10.1021/bi000593q. Further discussion of the ancestral ACE gene structure and evidence that the two active sites of human ACE have different functions.
Crackower MA, Sarao R, Oudit GY, Yagil C, Kozieradzki I, Scanga SE, Oliveira-dos-Santos AJ, da Costa J, Zhang L, Pei Y, et al: Angiotensin-converting enzyme 2 is an essential regulator of heart function. Nature. 2002, 417: 822-828. 10.1038/nature00786. The gene for ACE2 maps to a quantitative trait locus on the X chromosome in rat models of hypertension, and disruption of the gene results in severe cardiac dysfunction. Concomitant disruption of the ACE gene rescues cardiac function.
Wei L, Alhenc-Gelas F, Corvol P, Clauser E: The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J Biol Chem. 1991, 266: 9002-9008. This paper and  provide direct evidence that both catalytic domains of sACE are enzymatically active.
Jaspard E, Wei L, 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. 1993, 268: 9496-9503. Further evidence that both the N and C domains of sACE are catalytically active, but with different specificities.
Natesh R, Schwager SLU, Sturrock ED, Acharya KR: Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature. 2003, 421: 551-554. 10.1038/nature01370. The first crystal structure of a truncated version of human sACE.
Kim HM, Shin DR, Yoo OJ, Lee H, Lee J-O: Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril. FEBS Lett. 2003, 538: 65-70. 10.1016/S0014-5793(03)00128-5. After years of effort to obtain crystals of ACE, the crystal structure of Drosophila AnCE was published within weeks of that for human sACE.
Coates D: The angiotensin converting enzyme (ACE). Int J Biochem Cell Biol. 2003, 35: 769-773. 10.1016/S1357-2725(02)00309-6. A short review that examines the recently emerging factors underlying the therapeutic basis for ACE inhibition.
Ng KK, Vane JR: Fate of angiotensin I in the circulation. Nature. 1968, 218: 144-150. A classic analysis of angiotensin pharmacokinetics.
Rousseau A, Michaud A, Chauvet M-T, Lenfant M, 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. 1995, 270: 3656-3661. 10.1074/jbc.270.8.3656. The first report of a natural substrate for the N domain catalytic site of sACE.
Esther CR, Marino EM, Howard TE, Machaud A, Corvol P, Capecchi M, Bernstein KE: The critical role of tissue angiotensin-converting enzyme as revealed by gene targeting in mice. J Clin Invest. 1997, 99: 2375-2385. This paper describes the changes in renal structure that result from disrupting the C-domain of sACE.
Hagaman JR, Moyer JS, Bachman ES, Sibony M, Magyar PL, Welch JE, Smithies O, Krege JH, O'Brien DA: Angiotensin-converting enzyme and male fertility. Proc Natl Acad Sci USA. 1998, 95: 2552-2557. 10.1073/pnas.95.5.2552. Demonstration that sACE is essential for male fertility but that angiotensin I is not a necessary substrate.
Ramaraj P, Kessler SP, Colmenares C, Sen GC: Selective restoration of male fertility in mice lacking angiotensin-converting enzymes by sperm-specific expression of the testicular enzyme. J Clin Invest. 1998, 102: 371-378. The fertility defect in male ACE knockout mice is restored by selective expression of ACE only in sperm.
Turner AJ, Hooper NM: The angiotensin-converting enzyme gene family: genomics and pharmacology. Trends Pharmacol Sci. 2002, 23: 177-183. 10.1016/S0165-6147(00)01994-5. A review of the ACE gene family and an integrated analysis of the reninangiotensin system and its relationship to ACE2.
Tipnis SR, Hooper MN, Hyde R, Karran E, Christie G, Turner AJ: A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. J Biol Chem. 2000, 275: 33238-33243. 10.1074/jbc.M002615200. The first report of a homolog of human ACE that turns out to be a carboxypeptidase and tissue-specific. The authors refer to it as ACEH.
Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, Donovan M, Woolf B, Robison K, Jeyaseelan R, et al: A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ Res. 2000, 87: e1-e9. A report, almost concomitant with , on the identification of ACE2 and delineation of its enzymatic characteristics.
Matthews BW: Structural basis of the action of thermolysin and related zinc peptidases. Acc Chem Res. 1988, 21: 333-340. A classic review of the mechanism of action of the prototype zinc proteinase, thermolysin.
Zaman MA, Oparil S, Calhoun DA: Drugs targeting the renin-angiotensin-aldosterone system. Nat Rev Drug Discov. 2002, 1: 621-636. 10.1038/nrd873. An excellent summary of numerous clinical studies of drugs targeting one or more components of reninangiotensin-aldosterone system.
Bicket DP: Using ACE inhibitors appropriately. Am Fam Physician. 2002, 66: 461-468. A helpful review of the side-effects encountered with the use of ACE inhibitors.
Sleight P: The reninangiotensin system: a review of trials with angiotensin-converting enzyme inhibitors and angiotensin receptor blocking agents. Eur Heart J. 2002, 4 (Suppl A): A53-A57. A summary of clinical trials with ACE inhibitors and ACE receptor blockers.
Lonn E, Gerstein HC, Smieja M, Mann JFE, Yusuf S: Mechanisms of cardiovascular risk reductions with ramipril: insights from HOPE and HOPE substudies. Eur Heart J. 2003, 5 (Suppl A): A43-A48. How one ACE inhibitor, ramipril, can affect the risk of cardiovascular disease.
Adam A, Cagno M, Molinaro G, Perez M, Lepage Y, Agostoni A: Aminopeptidase P in individuals with a history of angio-oedema on ACE inhibitors. Lancet. 2002, 359: 2088-2089. 10.1016/S0140-6736(02)08914-6. A short summary of the incidence of angioedema as a side-effect of taking ACE inhibitors and the role of aminopeptidase P in the etiology of the disease.