Due to its action on angiotensin I and bradykinin, angiotensin converting enzyme (ACE, dipeptidyl carboxypeptidase, EC 3.4.15.1) plays a crucial role in blood pressure regulation [l]. Attention was focused on this enzyme when Lieberman observed elevated serum ACE levels in active sarcoidosis [2]. Because ACE is a sensitive index both in assessing the clinical status of this disease and in monit...

Two dipeptides, phenylalanylarginine (Phe-Arg) and serylproline (Ser-Pro), are released sequentially from bradykinin by angiotensin-converting enzyme purified from hog lungs; chloride increases the rate of release of both dipeptides. Using an automated ninhydrin-reagent method, we studied the kinetics of bradykinin hydrolysis. The reaction proceeded in the absence of chloride; however, the addi...

Introduction The outstanding role of polymorphonuclear granulocytes (PMN) to produce mediators of inflammation has been clearly established [2, 6–9]. After activation by extracellular stimuli the cells convert arachi-donic acid to three major groups of derivatives: the prostaglandins, the thromboxanes and the recently discovered leukotrienes are formed by oxygenation and further transformation....

Angiotensin converting enzyme (ACE) is a zinc-dependent dipeptidyl carboxypeptidase with an essential role in blood pressure homeostasis in mammals. ACE has long been targeted in the treatment of hypertension through ACE inhibitors, however current inhibitors are known to cause severe side effects. Therefore, there is a requirement for a new generation of ACE inhibitors and structural informati...

Human renal dipeptidase, an enzyme associated with glutathione metabolism and the hydrolysis of beta-lactams, is similar in sequence to a cluster of approximately 400 microbial proteins currently annotated as nonspecific dipeptidases within the amidohydrolase superfamily. The closest homologue to the human renal dipeptidase from a fully sequenced microbe is Sco3058 from Streptomyces coelicolor....

Glutathione is a tripeptide composed of glutamate, cysteine and glycine. Glutathione is present in millimolar concentrations in most mammalian cells and it is involved in several fundamental biological functions, including free radical scavenging, detoxification of xenobiotics and carcinogens, redox reactions, biosynthesis of DNA, proteins and leukotrienes, as well as neurotransmission/neuromod...

proteases (Mann, 1964). Some of them have been partially purified and charac¬ terized by Lundquist (1953), who described an aminopeptidase, which readily hydrolyses both diand tripeptides to leucylpeptides, without any preference. During recent years, however, several new chromogenic substrates have been introduced to the study of proteolytic activity (Nachlas, Goldstein & Seligman, 1962), and ...