140480-84-8

Basic information

• Product Name: Hippuric acid
• Synonyms: N-Benzoylglycine; [(phenylcarbonyl)amino]acetate; 2-benzamidoacetic acid; Bz-Gly-OH
• CAS NO: 140480-84-8
• Molecular Formula: C₉H₈NO₃
• Molecular Weight: 178.1653
• EINECS: 207-806-3
• Mol File: 140480-84-8.mol
• Article Data: 154

Chemical Properties

• Melting Point: 188-191℃
• Boiling Point: 464.1°C at 760 mmHg
• Flash Point: 234.5°C
• Vapor Pressure: 2.06E-09mmHg at 25°C
• CAS DataBase Reference: Hippuric acid(CAS DataBase Reference)
• NIST Chemistry Reference: Hippuric acid(140480-84-8)
• EPA Substance Registry System: Hippuric acid(140480-84-8)

Safety Data

• Safety Statements: S24/25:Avoid contact with skin and eyes.
• Hazardous Substances Data: 140480-84-8(Hazardous Substances Data)

Upstream product

• 19791-95-8 α-hydroxyhippuric acid 
• 1499-53-2 ethyl hippurate 
• 36701-37-8 silver(I) glycinate 
• 98-88-4 benzoyl chloride 
• 71-43-2 benzene 
• 93-97-0 benzoic acid anhydride 
• 56-40-6 glycine 
• 65-85-0 benzoic acid 
• 582-61-6 benzoyl azide 
• 501-52-0 3-Phenylpropionic acid 
• 1199-01-5 2-phenylazlactone 
• 1205-08-9 methyl hippurate 
• 5319-69-7 <<(Hydroxyimino)phenylmethyl>amino>essigsaeure 
• 959-22-8 p-nitrophenylbenzoate 

Downstream Products

• 5438-08-4 4-trans-cinnamylidene-2-phenyl-4H-oxazol-5-one 
• 35496-44-7 4-(3-oxo-3H-isobenzofuran-1-ylidene)-2-phenyl-4H-oxazol-5-one 
• 2644-92-0 2-phenyl-4-(1-phenyl-1H-pyrazol-4-ylmethylene)-4H-oxazol-5-one 
• 101445-44-7 N-[4-methyl-6-oxo-5-(5-oxo-2-phenyl-oxazol-2-ylidenemethyl)-1,6-dihydro-pyrimidin-2-yl]-acetamide 
• 75997-37-4 4-(1,5-dimethyl-3-oxo-2-phenyl-2,3-dihydro-1H-pyrazol-4-ylmethylene)-2-phenyl-4H-oxazol-5-one 
• 63670-26-8 4-fluoren-9-ylidene-2-phenyl-4H-oxazol-5-one 
• 102893-23-2 4-(2-acetoxy-3-methoxy-5-phenylazo-benzylidene)-2-phenyl-4H-oxazol-5-one 
• 101936-59-8 4-((Z)-4-acetoxy-3-methoxy-2-nitro-benzylidene)-2-phenyl-4H-oxazol-5-one 
• 855841-03-1 N-[(2-methoxy-phenyl)-(5-oxo-2-phenyl-4,5-dihydro-oxazol-4-yl)-methyl]-acetamide 

Relevant articles and documents

Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins

The angiotensin I-converting enzyme (ACE) inhibitory activities of protein hydrolysates prepared from cuttlefish (Sepia officinalis) proteins by treatment with various bacterial proteases were investigated. The hydrolysate generated by the crude enzyme from Bacillus mojavensis A21 displayed the highest ACE inhibitory activity, and the higher inhibition activity (87.11 ± 0.92% at 2 mg/mL) was obtained with hydrolysis degree of 16%. This hydrolysate was fractionated by size exclusion chromatography on a Sephadex G-25 into eight major fractions (P1-P8). Fraction P6, which exhibited the highest ACE inhibitory activity, was then fractionated by reversed-phase high performance liquid chromatography (RP-HPLC). Eleven ACE inhibitory peptides were isolated, and their molecular masses and amino acids sequences were determined using ESI-MS and ESI-MS/ MS, respectively. The structures of the most potent peptides were identified as Ala-His-Ser-Tyr, Gly-Asp-Ala-Pro, Ala-Gly-Ser-Pro and Asp-Phe-Gly. The first peptide displayed the highest ACE inhibitory activity with an IC50 of 11.6 μM. The results of this study suggest that cuttlefish protein hydrolysates are a good source of ACE inhibitory peptides.

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Effect of alkylamine on activity and stability of immobilized angiotensin converting enzyme

Angiotensin converting enzyme (ACE) was immobilized on chitosan microspheres with glutaraldehyde as cross-linking reagent. The activity and stability of immobilized ACE (I-ACE) were improved by further modification with alkylamines. The modification conditions were optimized. The characteristics of I-ACE and modified I-ACE (MI-ACE) including activity, kinetic parameters, optimal pH and temperature, stability and reusability were investigated. After modification, I-ACE activity was increased, Km decreased from 4.33 mM to 2.61 mM, optimal pH value was altered, pH stability, storage stability and thermal stability were improved, and optimal temperature did not change.

Interactions between Penicillin-Binding Proteins (PBPs) and Two Novel Classes of PBP Inhibitors, Arylalkylidene Rhodanines and Arylalkylidene Iminothiazolidin-4-ones

Several non-β-lactam compounds were active against various gram-positive and gram-negative bacterial strains. The MICs of arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones were lower than those of ampicillin and cefotaxime for methicillin-resistant Staphylococcus aureus MI339 and vancomycin-resistant Enterococcus faecium EF12. Several compounds were found to inhibit the cell wall synthesis of S. aureus and the last two steps of peptidoglycan biosynthesis catalyzed by ether-treated cells of Escherichia coli or cell wall membrane preparations of Bacillus megaterium. The effects of the arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-one derivatives on E. coli PBP 3 and PBP 5, Streptococcus pneumoniae PBP 2xS (PBP 2x from a penicillin-sensitive strain) and PBP 2xR (PBP 2x from a penicillin-resistant strain), low-affinity PBP 2a of S. aureus, and the Actinomadura sp. strain R39 and Streptomyces sp. strain R61 DD-peptidases were studied. Some of the compounds exhibited inhibitory activities in the 10 to 100 μM concentration range. The inhibition of PBP 2xS by several of them appeared to be noncompetitive. The dissociation constant for the best inhibitor (Ki = 10 μM) was not influenced by the presence of the substrate.

Direct measurement of the uncatalyzed rate of hydrolysis of a peptide bond

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Concise Modular Synthesis of Thalassotalic Acids A-C

The novel N-acyldehydrotyrosine analogues known as thalassotalic acids A-C were isolated from a marine bacterium by Deering et al. in 2016. These molecules were shown to have tyrosinase inhibition activity and thus are an attractive set of molecules for further study and optimization. To this end, a concise and modular synthesis has been devised and executed to produce thalassotalic acids A-C and two unnatural analogues. This synthesis has confirmed the identity and inhibitory data of thalassotalic acids A-C, more potent synthetic analogues (IC50 = 65 μM), and provides a route for further structure-activity relationship studies to optimize these molecules.

Preparation of asymmetric urea derivatives that target prostate-specific membrane antigen for SPECT imaging

Prostate-specific membrane antigen (PSMA) has been identified as a diagnostic and therapeutic target for prostate cancer. (S)-2-[3-[(R)-1-Carboxy- 2-mercaptoethyl]ureido-pentanedioic acid (Cys-CO-Glu) were used to design novel PSMA targeting probes by nucleophilic conjugate addition between cysteine and maleimide based reagents. 3 ([123I]IGLCE) was synthesized by this strategy and showed high affinity for PSMA. Results of binding inhibition assays of these derivatives suggested the importance of an aromatic group and succinimide moiety for high affinity. [123I]3 was evaluated in vivo with PSMA positive LNCaP and PSMA negative PC-3 human prostate cancer xenograft bearing mice. [125I]3 accumulated in LNCaP tumors but not in PC-3 tumors, and the accumulation was inhibited by 2-(phosphonomethyl)pentanedioic acid (2-PMPA). Use of [123I]3 provided positive images of LNCaP tumors in single photon emission tomography scans. These results warrant further evaluation of [123I]3 and its derivatives as radiolabeled probes for the diagnosis of prostate cancer.

Cyclodextrins to limit substrate inhibition and alter substrate selectivity displayed by enzymes

The substrate inhibition exhibited by carboxypeptidase A in catalysing the hydrolysis of (S)-2-O-(N-benzoylglycyl)β-phenyllactate) is limited by addition of cyclodextrins. The cyclodextrins do not significantly change the maximum rate of reaction, but they increase the concentration of the substrate at which the maximum rate of reaction is observed, by more than an order of magnitude when 0.105 mol dm-3 hydroxypropyl-β-cyclodextrin is used. Cyclodextrins also alter the substrate selectivity of α-chymotrypsin in catalysing the hydrolysis of (S)-N-acetylleucine methyl ester and (S)-N-acetylphenylalanine methyl ester, in favour of reaction of the former. Calculations show that these effects are due to complexation of the substrates by the cyclodextrins. Thus the results establish that cyclodextrins can be used to manipulate the concentrations Of enzyme substrates in free solution in a predictable manner.

Enzyme inhibitor screening by capillary electrophoresis with an on-column immobilized enzyme microreactor created by an ionic binding technique

A novel strategy for screening the enzyme inhibitors from the complex mixtures by capillary electrophoresis with an on-column immobilized enzyme microreactor created by an ionic binding technique is reported. The enzyme microreactor was prepared in two steps: First, the capillary wall was dynamically coated with a polycationic electrolyte hexadimethrine bromide (HDB) by simply flushing the column using the HDB solution. Subsequently, a plug of the enzyme solution was injected and incubated for 5 min to permit the enzyme molecules to immobilize on the positively charged coating via ionic binding. To demonstrate this strategy, angiotensin-converting enzyme (ACE) was employed as a model for the enzyme immobilization, inhibition study, and inhibitor screening. It has been proved that such a prepared immobilized ACE microreactor displays a high enough activity and stability. Furthermore, the immobilized enzyme microreactor could be easily renewed. The inhibition study or inhibitor screening was accomplished through the following procedure: (i) the substrate solution was injected and incubated within the microreactor for a short time span; (ii) subsequently, the voltage was applied to separate the product of the enzyme reaction from the unreacted substrate based on their different mobilities, the peak area of the product representing the enzyme activity; (iii) a certain amount of enzyme inhibitor or candidate compound was spiked into the substrate solution to assay the reduction of the immobilized enzyme activity. Thus, the inhibitors can be easily identified if the reduced peak area of the product is observed in electropherograms. Because the injection volume of the capillary was only 9.8 nL and the enzyme could be reusable, the assay cost could be dramatically reduced. The screening of a small compound library containing natural extracts and commercially available inhibitors was performed. The present approach has proved to be simple, rapid, and robust.

Enzymatic coupling of specific peptides at nonspecific ligation sites: Effect of Asp189Glu mutation in trypsin on substrate mimetic-mediated reactions

Two main drawbacks seriously restrict the synthetic value of proteases as reagents in peptide fragment coupling: (i) native proteolytic activity and, thus, risk of undesired peptide cleavage; (ii) limited enzyme specificities restricting the amino acid residues between which a peptide bond can be formed. While the latter can be overcome by the use of substrate mimetics achieving peptide bond formation at nonspecific ligation sites, the risk of proteolytic cleavage still remains and hinders the wide acceptance of this powerful strategy for peptide coupling. This paper reports on the effect of the trypsin point mutant Asp189Glu on substrate mimetic-mediated reactions. The effect of this mutation on the steady-state hydrolysis of substrate mimetics of the 4-guanidinophenyl ester type and on trypsin-specific Lys- and Arg-containing peptides was investigated. The results were confirmed by enzymatic coupling reactions using substrate mimetics as the acyl donor and specific amino acid-containing peptides as the acyl acceptor. The competition assay verifies the predicted shift in substrate preference from Lys and Arg to the substrate mimetics and, thus, from cleavage to synthesis of peptide bonds. The combination of results obtained qualifies the trypsin mutant D189E as the first substrate mimetic-specific peptide ligase.

A Facile Synthesis of 2-Aminopropane-1,2,3-tricarboxylic Acid and Its Symmetrical Dimethyl Ester

A new convenient synthetic route to 2-aminopropane-1,2,3-tricarboxylic acid is described. The first two stages of the threestep synthesis are performed in a one-pot procedure and include the cyclization of hippuric acid with DCC followed by treatment with methyl bromoacetate to yield an alkylated oxazolone. Its hydrolysis with HCl provides 2-aminopropane-1,2,3-tricarboxylic acid as its HCl salt. Esterification of the resulting acid with methanol in the presence of thionyl chloride leads selectively to its symmetrical diester.

Synthesis and evaluation of new phenyl acrylamide derivatives as potent non-nucleoside anti-HBV agents

As a continuation of our previous work, a series of new phenyl acrylamide derivatives (4Aa-g, 4Ba-t, 5 and 6a-c) were designed and synthesized as non-nucleoside anti-HBV agents. Among them, compound 4Bs could potently inhibit HBV DNA replication in wild-type and lamivudine (3TC)/entecavir resistant HBV mutant strains with IC50 values of 0.19 and 0.18 μM, respectively. Notably, the selective index value of 4Bs was above 526, indicating the favorable safety profile. Interestingly, unlike nucleoside analogue 3TC, 4Bs could significantly inhibit 3.5 kb pgRNA expression. Molecular docking study revealed that 4Bs could fit well into the dimer-dimer interface of HBV core protein by hydrophobic, π–π and H-bond interactions. Considering the potent anti-HBV activity, low toxicity and diverse anti-HBV mechanism from that of nucleoside anti-HBV agent 3TC, compound 4Bs might be a promising lead to develop novel non-nucleoside anti-HBV therapeutic agents, and warranted further investigation.

Design, synthesis and anti-inflammatory/analgesic evaluation of novel di-substituted urea derivatives bearing diaryl-1,2,4-triazole with dual COX-2/sEH inhibitory activities

Herein, two novel series of diaryl-1,2,4-triazole hybrid to amide conjugates (5a-e) or urea conjugates (10a-f) have been synthesized followed by in vitro evaluation against cyclooxygenase-2/soluble epoxide hydrolase (COX-2/sEH) enzymes using ELISA enzyme assays. In vivo analgesic and anti-inflammatory activities for the new compounds have been carried out using the reported animal protocols. The preliminary results revealed that compounds 10e and 10c were the most active compounds against both COX-2/sEH enzymes (COX-2 IC50 = 1.98 μM and 2.13 μM; sEH = 1.09 and 1.23 nM, respectively). Moreover, the in vivo screening assays confirmed their superiority compared to the other derivatives by exhibiting higher anti-inflammatory and analgesic activity (91.27 and 89.32% edema inhibition; 55.97–50.00% writhing inhibition, respectively) than celecoxib (88.30% edema inhibition; 13.43% writhing inhibition). Collectively, compounds 10e and 10c can be considered as promising dual COX-2/sEH inhibitors with expected less cardiovascular adverse effects affording good anti-inflammatory and analgesic leads for further optimization.