Biological and biochemical properties of angiotensin-converting enzyme

Soffer, Richard L.; Das, Manjusri; Caldwell, P. R. B.; Seegal, Beatrice Carrier; Hsu, Konrad C.

doi:10.1007/bf01973275

Cited by 6 publications

(3 citation statements)

References 27 publications

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“…Dipeptidylcarboxypeptidase (DCP)/peptidyl dipeptidase, first described in E. coli cleaves dipeptides of the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetra peptides [29]. In the mammalian system, the same function is performed by peptidyl dipeptidase A, also known as angiotensin converting enzyme (ACE) [30]. LdDCP belongs to the zinc metallopeptidase family and cleaves N-benzoyal-L-glycyl-L-histidyl-L-leucine (HHL), a substrate for ACE as well as bacterial DCP to release hippuric acid [6].…”

Section: Resultsmentioning

confidence: 99%

Characterization of dipeptidylcarboxypeptidase of Leishmania donovani: a molecular model for structure based design of antileishmanials

Baig

Kumar

Siddiqi

et al. 2009

J Comput Aided Mol Des

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Leishmania donovani dipeptidylcarboxypeptidsae (LdDCP), an angiotensin converting enzyme (ACE) related metallopeptidase has been identified and characterized as a putative drug target for antileishmanial chemotherapy. The kinetic parameters for LdDCP with substrate, Hip-His-Leu were determined as, Km, 4 mM and Vmax, 1.173 micromole/ml/min. Inhibition studies revealed that known ACE inhibitors (captopril and bradykinin potentiating peptide; BPP1) were weak inhibitors for LdDCP as compared to human testicular ACE (htACE) with Ki values of 35.8 nM and 3.9 microM, respectively. Three dimensional model of LdDCP was generated based on crystal structure of Escherichia coli DCP (EcDCP) by means of comparative modeling and assessed using PROSAII, PROCHECK and WHATIF. Captopril docking with htACE, LdDCP and EcDCP and analysis of molecular electrostatic potentials (MEP) suggested that the active site domain of three enzymes has several minor but potentially important structural differences. These differences could be exploited for designing selective inhibitor of LdDCP thereby antileishmanial compounds either by denovo drug design or virtual screening of small molecule databases.

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Section: Resultsmentioning

confidence: 99%

Characterization of dipeptidylcarboxypeptidase of Leishmania donovani: a molecular model for structure based design of antileishmanials

Baig

Kumar

Siddiqi

et al. 2009

J Comput Aided Mol Des

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“…Die bereits unter physiologischen Bedingungen hohe ACE-Aktivit~it in den pulmonalen Kapillarendothelien wandelt das anflutende Angiotensin I wfihrend einer Lungenperfussion offensichtlich vollst~indig in Angiotensin II um [10,15,20]. Deshalb ist eine wesentliche Beeinflussung der Angiotensin II-Konzentration, der wichtigsten physiologisch wirksamen Komponente des Renin-Angiotensin-Systems, durch die verfinderte ACE-Aktivit/it bei Sarkoidose unwahrscheinlich.…”

Section: I S K U S S I O Nunclassified

Die Bedeutung des Angiotensin I-Converting-Enzyms f�r die Diagnose einer Sarkoidose

Baur¹,

Fruhmann²,

König³

et al. 1980

Klin Wochenschr

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Serum ACE activity measured fluorimetrically was found to be 2.95 +/- (SD) 1.76 mu mol/ml x h in 31 untreated patients with sarcoidosis. It was significantly elevated (p less than 0.001) in comparison to 38 healthy controls 0.97 +/- (SD) 0.30 mu mol/ml x h), 81 subjects with miscellaneous lung diseases, 20 corticosteroid treated patients with sarcoidosis and 15 subjects with resolved sarcoidosis. Resolution of sarcoidosis spontaneously or induced by corticosteroids was accompanied in all 17 cases by a decrease of serum ACE activity, in most cases, to normal values. On the other hand 7 out of 9 untreated patients with a chronic course of sarcoidosis did not show a comparable change of ACE. Our results reveal a close relationship between the activity of the disease and the level of ACE in the serum. The determination of the serum activity of ACE and its variations with time is quite useful in the diagnosis and follow-up of sarcoidosis and contributes to a further restriction of necessary operative procedures in the diagnosis of sarcoidosis.

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“…It has recently been found that pure CE is also a metalloenzyme containing one atom of zinc [8]. However, CE is not readily inhibited by 2-ME.…”

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confidence: 99%

Inactivation of bradykinin in the pulmonary circulation

Stewart

1976

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Bradykinin is very efficiently inactivated on passage through the pulmonary circulation by enzymes on the vascular walls. Several different cleavages of the bradykinin molecule have been observed; one appears to be due to angiotensin converting enzyme. Several types of inhibitors have been useful in the study of these pulmonary peptidases and have helped increase understanding of the functioning of the angiotensin and plasma kinin systems.

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Biological and biochemical properties of angiotensin-converting enzyme

Cited by 6 publications

References 27 publications

Characterization of dipeptidylcarboxypeptidase of Leishmania donovani: a molecular model for structure based design of antileishmanials

Characterization of dipeptidylcarboxypeptidase of Leishmania donovani: a molecular model for structure based design of antileishmanials

Die Bedeutung des Angiotensin I-Converting-Enzyms f�r die Diagnose einer Sarkoidose

Inactivation of bradykinin in the pulmonary circulation

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