Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.15.1 (ACE)
 18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The occurrence of angiotensin converting enzyme (EC 3.4.15.1; ACE) was demonstrated for the first time in serum of newt (Triturus carnifex) and frog (Rana esculenta). The enzymatic activity was evidenced following hydrolysis of N-[3-(2-furyl) acryloyl]L-phenylalanyl glycyl glycine (FAPGG), a synthetic substrate of ACE. The serum enzyme liberated N-[3-(2-furyl) acryloyl]L-phenylalanine (FAP) from FAPGG. The properties of the amphibian serum enzymes were compared with those of swine. The amphibian serum FAPGG hydrolysing activities were inhibited by typical ACE inhibitors, captopril and lisinopril. The optimum of pH was 8.3 at 10 and 37 degrees C and the temperature optimum was 45 degrees C. The values were similar to those of swine serum. The FAPGG Michaelis-Menten constants (K(m)) at 37 degrees C of amphibian serum enzymes (0.337 mM and 0.282 mM for frog and newt, respectively) were lower than that of swine (1.305 mM), but close to human serum enzyme. The K(m) values obtained at 10 degrees C were lower than those at 37 degrees C (0.152, 0.086, and 1.029 mM for frog, newt, and swine serum, respectively). Amphibian sera hydrolysed bullfrog synthetic angiotensin I to produce angiotensin II. Captopril (50 microM) inhibited the production of angiotensin II.
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PMID:Presence of angiotensin converting enzyme (ACE) activity in serum of amphibian: comparison with ACE activity of mammalian serum. 924 91

For determination of levels of plasmatic inhibitor of ACE (angiotensin convertase) a simple method was used based on a combination of enzymatic reaction followed by an HPLC determination of its product. The inhibitor (e.g. enalaprilat) was at first separated from the biological material by deproteination (methanol). Then, an aliquot of the sample was added to the reaction mixture containing a commercial ACE enzyme, its specific substrate FAPGG (N-(3-[2-furyl]acryloyl)-Phe-Gly-Gly) and buffer (Tris--HCl, pH 7.5). Degree of inhibition of the conversion of this substrate to FAP (desGlyGlyFAPGG) by the inhibitor present in the sample is related to its amount by a simple dose-response relationship. The amount of the FAP was determined by an HPLC on a RP-18 column with an acetonitril--nonylamine buffer (pH 2.4, adjusted with phosphoric acid) as a mobile phase with detection at 305 nm. Alternatively, the activity of the endogenous ACE present in the plasma was measured. The substrate FAPGG was added to the plasmatic sample containing both the inhibitor and endogenous ACE (as the sample was not deproteinized in this case) and the reaction product was determined as above. Inhibitor concentration has been obtained from a dose--response curve expressing the interaction with inhibitor with an ACE enzyme.
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PMID:Determination of enzyme (angiotensin convertase) inhibitors based on enzymatic reaction followed by HPLC. 1124 13

Angiotensin-I-converting enzyme (ACE, EC 3.4.15.1) plays a central role in the regulation of blood pressure in man. The objective of this study was to evaluate and modify the furanacryloyl-L-phenylalanylglycylglycine (FAPGG) assay method for quantification of ACE activity. The fixed time conditions developed for assay of ACE activity were as follows: 0.8 mM FAPGG, 175 + or - 10 units l(-1) ACE, incubation at 37 degrees C for 30 min and enzyme inactivation with 100 mM ethylenediaminetetra-acetic acid (EDTA). Hydrolysis of FAPGG to FAP and GG was quantified by measuring the decrease in absorbance at 340 nm. It was shown that increasing the level ACE activity in the assay from 155 to 221 + or - 15 units l(-1) resulted in a corresponding increase in the apparent IC(50) value for Captopril from 9.10 to 39.40 nM. Similar trends in the apparent IC50 values for a whey protein hydrolysate were obtained. The results demonstrate the requirement for carefully controlling ACE activity levels in the assay in order to obtained comparable and reproducible values for the inhibitory potency of ACE inhibitors.
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PMID:Modification of the furanacryloyl-L-phenylalanylglycylglycine assay for determination of angiotensin-I-converting enzyme inhibitory activity. 1516 24