500-98-1

Usage

Chemical Properties

White Solid

Uses

A metabolite of carboxylic acid.

Definition

ChEBI: A N-acylglycine that is glycine substituted on nitrogen with a phenylacetyl group.

InChI:InChI=1/C10H11NO3/c12-9(11-7-10(13)14)6-8-4-2-1-3-5-8/h1-5H,6-7H2,(H,11,12)(H,13,14)/p-1

Upstream product

• 99-87-6 4-methylisopropylbenzene 
• 15545-34-3 methyl benzylpenillonate 
• 23776-85-4 N-(phenylacetyl)oxysuccinimide 
• 56-40-6 glycine 
• 103-82-2 phenylacetic acid 
• 15440-31-0 2-benzylidene-2H-oxazol-5-one 
• 5467-51-6 N-(cyanomethyl)-2-phenylacetamide 
• 28268-03-3 N-Carboxymethyl-phenylessigsaeure-amidoxim 
• 103-80-0 phenylacetyl chloride 
• 123910-63-4 tert-butyl (2-phenylacetyl)glycinate 
• 872808-70-3 phenylthioacetylglycine 
• 7732-18-5 water 
• 60-29-7 diethyl ether 
• 93769-19-8 3-(Phenylmethyl)-4H-1,2,4-oxadiazin-6(5H)-on 

Downstream Products

• 5259-87-0 methyl 2-(2-phenylacetamido)acetate 
• 4838-35-1 N-(phenylacetyl)glycine ethyl ester 
• 63257-00-1 N-(p-nitrophenylacetyl)-glycine 
• 15440-34-3 N-benzyl-2-(2-phenylacetamido)acetamide 
• 412035-63-3 acetoxy-(2-phenyl-acetylamino)-methane 
• 5874-59-9 N-phenylacetyl-glycine-anhydride 
• 100063-44-3 3-acetyl-2-benzyliden-oxazolidin-5-one 
• 61369-26-4 2-benzyl-4-ethoxymethylene-5-oxazolone 
• 66591-90-0 N-phenylacetyl-glycine phenyl ester 
• 1431-98-7 6β-[(N-phenylacetyl-glycyl)-amino]-penicillanic acid 
• 17080-27-2 N-phenylacetyl-glycine 4-nitro-phenyl ester 

Relevant academic research and scientific papers

GRANZYME B DIRECTED IMAGING AND THERAPY

Provided herein are heterocyclic compounds useful for imaging Granzyme B. Methods of imaging Granzyme B, combination therapies, and kits comprising the Granzyme B imaging agents are also provided.

Development of a new enzyme-responsive self-immolative spacer conjugate applicable to the controlled drug release

A new self-immolative spacer conjugate based on a chemical adaptor unit aiming at controlled releasing drugs was designed and synthesized. It releases a fluorophore which was used as a model drug via a spontaneous cyclization mechanism after cleavage of an enzyme substrate. This system was proved to be stable under physiological conditions and only decomposed triggered by enzyme. It provides a generic linkage allowing connection of a variety of drugs and targeted devices to the chemical adaptor.

Thermodynamics of phenylacetamides synthesis: Linear free energy relationship with the pK of amine

The effective equilibrium constants K′C expressed through the total concentrations of the reagents for the synthesis of N-phenylacetyl-derivatives in aqueous medium from phenylacetic acid and various primary amino compounds have been determined with penicillin acylase as a catalyst. Broad specificity of penicillin acylase (EC 3.5.1.11) to amino components made possible to investigate the acylation of primary amines with different structures and physicochemical properties. Analysis of different components of the effective standard Gibbs energy change ΔGC o′ has revealed favorable thermodynamics for the synthesis of phenylacetamides from unionized substrates forms, however the ionization of reactants carboxy and amino groups in aqueous solutions pushes the equilibrium position to the hydrolysis especially in case of highly basic amines. A linear correlation between the standard Gibbs energy change for amide bond formation from the unionized reagents species and the basicity of amino group was observed: ΔGTo=-3.56pKamine+7.71(kJ/mol). The established linear free energy relationship (LFER) allows to predict the thermodynamic parameters for direct condensation of phenylacetic acid with any amine of known pK. Condensation of phenylacetic acid and amines with pK value within 1.5-8.5 was shown to be thermodynamically favorable in homogeneous aqueous solution. .

Novel synthesis and characterization of some new-2-(R) phenyl- 4-(-4-bromo-2-fluoro benzylidene)-oxazol-5-ones

In the present study a series of some new 2-(substituted) phenyl- 4-(4-bromo-2-fluoro benz-ylidene)-oxazol-5-ones (2a-2j) were synthesized by the condensation of selected substituted benzoyl glycine (1a-1j) with 4-bromo-2-fluoro benzaldehyde in the presence of fused sodium acetate and acetic anhydride. The constitution of the newly synthesized compounds has been supported by their physical properties, elemental analysis, colour, m.p, IR spectral analysis data.

The synthesis and in vitro testing of structurally novel antibiotics derived from acylnitroso Diels-Alder adducts

The structural similarity between β-lactam antibiotics, such as penicillin, and isoxazolidine-3,5-dicarboxylic acids led to the hypothesis that isoxazolidine-3,5-dicarboxylic acids could be effective analogs of β-lactam antibiotics. The syntheses of relevant isoxazolidine-3,5-dicarboxylic acids from acylnitroso Diels-Alder adducts and subsequent biological testing have shown that these first examples are inhibitors of Escherichia coli X580.

The use of cellulose (chromatography paper) as a cheap, versatile and non-covalent support for organic molecules during multi-step synthesis

Cellulose chromatography paper provides a novel non-covalent support for synthesis and in-situ purification of multi-dimensional arrays.

Inverse acyl phosph(on)ates: Substrates or inhibitors of β-lactam-recognizing enzymes?

Acyl phosph(on)ates represent a new class of inhibitors of β-lactam - recognizing enzymes. Previously described members of this class were aroyl phosph(on)ates. These compounds have been shown to acylate and/or phosphylate the active site serine residue, leading to either transient or essentially irreversible inhibition [Li, N., and Pratt, R. F. (1998) J. Am. Chem. Soc. 120, 4264-4268]. The present paper describes the synthesis and evaluation as inhibitors of an inverse pair of acyl phosph(on)ates that incorporate the amido side chain that represents a major substrate specificity determinant of these enzymes. Thus, N-(phenylacetyl)glycyl phenyl phosphate and benzoyl N-(benzyloxycarbonyl)aminomethyl phosphonate were prepared. The former of these compounds was found to be a substrate of typical class A and C β-lactamases and of the DD-peptidase of Streptomyces R61; it thus acylates the active site serine. In contrast, the latter compound was an irreversible inhibitor of the above enzymes, probably by phosphonylation of the active site serine. With each of these enzymes therefore, the amido side chain rather than the acyl group dictates the orientation of the bound phosph(on)ate and thus the mode of reaction.

ERYTHROMYCIN A 9-0-OXIME DERIVATIVES ENDOWED WITH ANTIBIOTIC ACTIVITY

PCT No. PCT/EP95/04815 Sec. 371 Date May 16, 1997 Sec. 102(e) Date May 16, 1997 PCT Filed Dec. 7, 1995 PCT Pub. No. WO96/18633 PCT Pub. Date Jun. 20, 1996Erythromycin 9-oxime derivatives wherein a phenyl or heterocylic group is attached indirectly to the 9-position of erythromycin A through an alkylene diamine bridging member. These compounds exhibit broad spectrum antibiotic activity.

The pH-rate profile for the hydrolysis of a peptide bond

The rate of hydrolysis of N-(phenylacetyl)glycyl-D-valine (PAGV), an acyclic penicillin G analogue, at pH 0, 1, 3, 5, 7, 9, 11, 13, and 14 has been measured at 37 °C and a pH-rate profile constructed. At each pH, hydrolysis of both the (phenylacetyl)glycyl amide bond and glycyl-D-valine peptide bond was monitored. At pH 3, 5, 7, 9, and 11, the hydrolysis products glycyl-D-valine and D-valine were derivatized with naphthalene-2,3-dialdehyde in the presence of cyanide; the resultant 1-cyano-2-substituted- benz[f]isoindole (CBI) derivatives, which are highly fluorescent, were then quantified using reverse-phase HPLC. The hydrolysis reactions were explicitly shown to be first-order peptide concentration at pH 5 and 9, and all rates were shown to be independent of the buffer concentration. The rates at pH 0, 1, 13, and 14 were measured in 1 M DCl, 0.1 M DCl, 0.1 M NaOD, and 1 M NaOD, respectively, and the hydrolysis products were detected by 1H NMR. The first-order rate constants obtained from the above reactions were fit to the general equation k = k(H2O) + k(H)3(O) [H3O+] + k(OH)-[OH-] to yield the following results: for hydrolysis of the (phenylacetyl)glycyl bond, k(H2O) = (9.05 ± 6.36) x 10-11 s-1, k(H3O)+ = (1.60 ± 1.04) x 10-6 M-1 s-1, and k(OH)- = (1.11 ± 0.73) x 10-6 M-1 s-1; and for hydrolysis of the glycyl-D-valine bond, k(H2O) = (8.23 ± 4.33) x 10-11 s-1, k(H3O)+ = (1.67 ± 0.80) x 10-6 M-1 s-1, and k(OH)- = (1.16 ± 0.56) x 10-6 M-1 s-1. At pH 7, the hydrolysis of both the (phenylacetyl)glycyl amide bond and glycyl-D-valine peptide bond is dominated by k(H2O). The corresponding half-life for (phenylacetyl)glycyl bond hydrolysis is 243 years (with a range of 143-817 years within experimental error), while that for glycyl-D-valine bond hydrolysis is 267 years (with a range of 175-564 years).

Derivatives of L-proline, their preparation and their biological uses

The L-proline derivatives of the invention correspond to the Formula I: STR1 in which R1 corresponds to the Formula II: STR2 in which R is a carbonyl group, an acyl group --Y--CO-- or an oxy-acyl group --O--Y--CO--, Y being an alkyl or an alkenyl chain, Z being one or more hydrogen atoms, or one or more substituents chosen from among halogen atoms, CF3, alkyl or alkoxy groups and an alkylenedioxy group in the case of two neighbouring substituents, R2 is --NH2, --OH, or a derivative of these groups, A1 and A2 are amino acid residues and B1 and B2 represents a hydrogen atom or a methyl group, and the pharmacologically acceptable salts of these derivatives. These derivatives are useful particularly as the active principles of medicines possessing, in particular, a nootropic action.