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

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

Hippuryl-His-Leu-OH hydrate (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 hydrate (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 hydrate 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 hydrate, 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 (free acid)

C₂₁H₂₇N₅O₅.xH₂O

207386-83-2

Solid

White to off-white

Room temperature in continental US; may vary elsewhere.

Sealed storage, away from moisture

*In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture)

• [1]. Komolafe K, et al. African locust bean (Parkia biglobosa, Jacq Benth) leaf extract affects mitochondrial redox chemistry and inhibits angiotensin-converting enzyme in vitro[J]. Clinical Phytoscience, 2017, 3(1): 19.

  [2]. Inoue K, et al. Screening assay of angiotensin-converting enzyme inhibitory activity from complex natural colourants and foods using high-throughput LC-MS/MS. Food Chem. 2011 Jun 15;126(4):1909-15.  [Content Brief]

  [3]. Babić N, et al. Angiotensin converting enzyme activity in compensatory renal hypertrophy. Bosn J Basic Med Sci. 2007 Feb;7(1):79-83.  [Content Brief]