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Application Area

Benzoyl-L-alanine methyl ester

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

L-Amino Acids

Catalog number

BAT-003889

CAS number

7244-67-9

Molecular Formula

C11H13NO3

Molecular Weight

207.20

IUPAC Name

methyl (2S)-2-benzamidopropanoate

Synonyms

Bz-L-Ala-Ome; Methyl N-benzoyl-L-alaninate

Appearance

White powder

Purity

≥ 99% (TLC)

Density

1.131 g/cm3

Melting Point

61-63 °C

Boiling Point

346.25°C (rough estimate)

Storage

Store at 2-8 °C

InChI

InChI=1S/C11H13NO3/c1-8(11(14)15-2)12-10(13)9-6-4-3-5-7-9/h3-8H,1-2H3,(H,12,13)/t8-/m0/s1

InChI Key

QRDFLIILGVFYCF-QMMMGPOBSA-N

Canonical SMILES

CC(C(=O)OC)NC(=O)C1=CC=CC=C1

Benzoyl-L-alanine methyl ester, a versatile compound with diverse applications in bioscience, is utilized across various domains. Here are the key applications presented with a high degree of perplexity and burstiness:

Pharmaceutical Synthesis: Acting as an intermediary in pharmaceutical synthesis, Benzoyl-L-alanine methyl ester plays a pivotal role in the creation of drugs targeting specific biological pathways. This compound serves as a precursor for developing new medications with enhanced efficacy and minimized side effects, propelling advancements in drug discovery and delivery.

Peptide Research: Within the realm of peptide synthesis, Benzoyl-L-alanine methyl ester finds application in research endeavors. By integrating this compound into peptide chains, researchers can delve into protein interactions and functionalities, a crucial step in unraveling disease mechanisms and devising novel therapeutic approaches, shedding light on the intricate workings of biological systems.

Biocatalysis: Engaging in enzymatic reactions, Benzoyl-L-alanine methyl ester aids in the production of enantiomerically pure compounds, essential in generating chiral molecules significant for the pharmaceutical industry. This involvement in biocatalysis is instrumental in crafting more potent and selective drugs, driving progress in drug development and efficacy.

Chemical Analysis: In the realm of analytical chemistry, Benzoyl-L-alanine methyl ester serves as a standard reference compound, contributing to the calibration of instruments and validation of analytical techniques. This application ensures precision and dependability in detecting and quantifying various substances in research and clinical environments, bolstering the accuracy and reliability of analytical findings.

1. [Structure of the active center of subtilisin 72]

N F Kazanskaia, O A Kost Biokhimiia. 1982 May;47(5):834-41.

The inhibition by N-benzoyl-L-arginine of subtilisin-catalyzed hydrolysis of various substrates was investigated. Study of combined hydrolysis of these substrates revealed the existence of two productive binding sites in the subtilisin 72 molecule. The type of substrate adsorption depends on the nature of the acyl moiety of the molecule and on the nature of the split-off group. The N-acetyl-L-tyrosine ethyl ester and N-benzoyl-L-citrulline methyl ester are bound at the same adsorption site (A), while N-cinnamoyl imidazole and N-acetyl-L-valine methyl ester are found at another adsorption site (B); N-benzoyl-L-alanine methyl ester can be adsorbed both at site A and at site B. However, substitution of the split-off group in the substrates previously adsorbed at site B by the p-nitrophenyl group causes their transfer to site A.

2. Kinetic anomalies in chymotryptic hydrolyses of p-nitrophenyl acetate and N-benzoyl-L-alanine methyl ester

D Nohara, M Wakamatsu, M Goto, T Sakai Chem Pharm Bull (Tokyo). 1989 Jul;37(7):1685-90. doi: 10.1248/cpb.37.1685.

Kinetic and thermodynamic parameters were evaluated for the acylation and the deacylation steps in the hydrolysis of p-nitrophenyl acetate by alpha-chymotrypsin at pH 7.8 and at temperatures between 15 and 35 degrees C by the use of stopped-flow and ordinary ultraviolet spectrophotometers. In contrast to the temperature dependencies of k2 and Ks reported in the literature (P.A. Adams and E.R. Swart, Biochem. J., 161, 83 (1977], no kinetic anomaly was observed in either of the steps, but reasonable straight lines were obtained in both Arrhenius and van't Hoff plots. On the other hand, in the chymotryptic hydrolysis of N-benzoyl-L-alanine methyl ester a sharp kinetic anomaly was found. The discrepancy in the case of p-nitrophenyl acetate is discussed in connection with a possible conformational change of the enzyme, an alteration of the rate-limiting step or differences in the experimental procedures. The cause of the anomaly observed in the case of N-benzoyl-L-alanine methyl ester is also discussed in detail.

3. Purification and properties of elastolytic enzyme from Flavobacterium immotum

H Ozaki, I Shiio J Biochem. 1975 Jan 1;77(1?):171-80.

Elastolytic enzyme was purified and crystallized from culture fluid of Flavobacterium immotum No. 9-35. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis. The molecular weight was determined by Sephadex G-100 gel filtration to be 13,000. The isoelectric point was between pH 8.3 and 8.9. The optimum pH of the enzyme was 7.2 for elastolytic activity. The purified enzyme showed not only elastolytic activity, but also non-specific proteolytic activity against various other proteins. Milk-clotting activity was also observed. The enzyme did not act on keratin, collagen, or fourteen amino acid esters, including N-benzoyl-L-alanine methyl ester, N-benzoyl-L-arginine ethyl ester, and N-acetyl-L-tyrosine ethyl ester, which were typical substrates of pancreatic elastase [EC 3.4.21.11], trypsin [EC 3.4.21.4], and chymotrypsin [EC 3.4.21.1], respectively. However, the enzyme selectively hydrolyzed elastin when both elastin and albumin were present in the reaction mixture. The enzyme was inhibited by o-phenanthroline and various heavy metals such as cadmium, lead, zinc, and mercury. Various inhibitors, such as diisopropyl phosphofluoridate, tosyl-L-lysine chloromethyl ketone, tosyl-L-phenylalanine chloromethyl ketone, trypsin inhibitor, iodoacetamide, etc., had no effect on the elastolytic activity.