Hippuryl-His-Leu-OH  (Synonyms: N-Benzoyl-Gly-His-Leu)

Hippuryl-His-Leu-OH (N-Benzoyl-Gly-His-Leu) is a specific substrate for angiotensin-converting enzyme (ACE I) and a molecular tool used for ACE activity detection in in vitro experiments. Hippuryl-His-Leu-OH is hydrolyzed by ACE through competitive binding. Under ACE catalysis, Hippuryl-His-Leu-OH undergoes hydrolysis to produce hippuric acid (HA). The amount of HA produced can be used to quantitatively assess ACE activity or screen for ACE inhibitors. The released His-Leu can also react with o-phthalaldehyde or Fluorescamine (HY-D0715) for fluorescence detection. Hippuryl-His-Leu-OH can be applied to the in vitro screening of ACE inhibitors for hypertension and cardiovascular diseases, and is also used in the study of ACE activity changes in physiological and pathological processes such as renal compensatory hypertrophy^[1][2][3].

Hippuryl-His-Leu-OH (8.3 mM; incubated with the enzyme source for 15 minutes, then incubated with the substrate for 30 minutes) can be hydrolyzed by angiotensin-converting enzyme (ACE) to produce hippuric acid. The ACE inhibitory activity of substances such as Parkia biglobosa extract can be evaluated by detecting the amount of hippuric acid produced^[1].
Hippuryl-His-Leu-OH (1 mM, 0.1 mM; incubated at 37°C for 150 min) as an ACE-specific substrate, its hydrolyzed product, hippuric acid, after solid-phase extraction (SPE) treatment, can be quantitatively detected by LC/SID-ESI-MS/MS technology, enabling efficient screening of ACE inhibitors in complex natural pigments and foods^[2].
Hippuryl-His-Leu-OH is used as a substrate for spectrophotometric detection of ACE activity in serum and tissues. The generated hippuric acid has a characteristic absorption peak at 228 nm, which reflects the catalytic activity level of ACE^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

In a unilateral nephrectomy-induced compensatory renal hypertrophy model in Wistar rats, Hippuryl-His-Leu-OH, as a specific substrate for angiotensin-converting enzyme (ACE), is hydrolyzed in an enzymatic reaction to produce hippuric acid. The amount of hippuric acid produced can be used to quantify serum and renal tissue ACE activity. The results showed that 7 days after unilateral nephrectomy, serum ACE activity in rats was significantly increased, and renal tissue ACE activity was significantly increased by 23%^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

429.47

C₂₁H₂₇N₅O₅

31373-65-6

Hippuryl-His-Leu-OH

Hippuryl-HL-OH

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Nishimura K, et al. Purification of angiotensin I-converting enzyme from human lung. Biochim Biophys Acta. 1977 Aug 11;483(2):398-408.  [Content Brief]

  [2]. Santos RA, et al. An improved fluorometric assay of rat serum and plasma converting enzyme. Hypertension. 1985 Mar-Apr;7(2):244-52.  [Content Brief]

  [3]. Horiuchi M, et al. Method for determination of angiotensin-converting enzyme activity in blood and tissue by high-performance liquid chromatography. J Chromatogr. 1982 Dec 10;233:123-30.  [Content Brief]