28047-15-6

Basic information

• Product Name: PHENYLAC-GLN-OH
• Synonyms: PHENYLAC-GLN-OH;2-[[2-(4-hydroxyphenyl)acetyl]amino]pentanedioic acid;4-Hydroxyphenylacetylglutamine;(2S)-4-carbamoyl-2-[(2-phenylacetyl)amino]butanoic acid;alpha-N-Phenylacetyl-L-glutamine;Glutamine, N2-(phenylacetyl)-, L- (8CI);phenylacetylglutamine;N2-(Phenylacetyl)glutamine
• CAS NO: 28047-15-6
• Molecular Formula: C₁₃H₁₆N₂O₄
• Molecular Weight: 264.28
• Product Categories: Amino Acids & Derivatives;Aromatics;Intermediates & Fine Chemicals;Pharmaceuticals
• Mol File: 28047-15-6.mol
• Article Data: 3

Chemical Properties

• Melting Point: 85-87?C
• Boiling Point: 655.5 °C at 760 mmHg
• Flash Point: 350.2 °C
• Appearance: /
• Density: 1.279
• Vapor Pressure: 1.33E-17mmHg at 25°C
• Refractive Index: 1.595
• Storage Temp.: Store at 0-5°C
• Solubility: DMSO (Slightly), Methanol (Slightly)
• PKA: 3.40±0.10(Predicted)
• CAS DataBase Reference: PHENYLAC-GLN-OH(CAS DataBase Reference)
• NIST Chemistry Reference: PHENYLAC-GLN-OH(28047-15-6)
• EPA Substance Registry System: PHENYLAC-GLN-OH(28047-15-6)

Safety Data

• Hazardous Substances Data: 28047-15-6(Hazardous Substances Data)

Usage

Chemical Properties

PHENYLAC-GLN-OH is White Solid

Uses

Different sources of media describe the Uses of 28047-15-6 differently. You can refer to the following data:
1. It is used as biomarker for metabolic age.
2. PHENYLAC-GLN-OH is used as biomarker for metabolic age.

InChI:InChI=1/C13H15NO6/c15-9-3-1-8(2-4-9)7-11(16)14-10(13(19)20)5-6-12(17)18/h1-4,10,15H,5-7H2,(H,14,16)(H,17,18)(H,19,20)

Synthetic route

D-Glutamin (5959-95-5) + phenylacetyl chloride (103-80-0) → α-N-phenylacetyl-L-glutamine (28047-15-6)

Conditions	Yield
With sodium hydrogencarbonate

GLUTAMINE (56-85-9, 585-21-7, 5959-95-5, 6899-04-3) + benzeneacetic acid methyl ester (101-41-7) → D-Glutamin (5959-95-5) + α-N-phenylacetyl-L-glutamine (28047-15-6)

Conditions	Yield
With sodium hydroxide; E. coli penicillin-G acylase F24A mutant at 25℃; pH=9.0;

sulfuric acid (7664-93-9) + α-N-phenylacetyl-L-glutamine (28047-15-6) → phenylacetic acid (103-82-2) + D-Glutamic acid (6893-26-1)

α-N-phenylacetyl-L-glutamine (28047-15-6) + aq. barium hydroxide solution → barium salt of/the/ phenacetyl-d-glutamic acid

Upstream product

• 5959-95-5 D-Glutamin 
• 103-80-0 phenylacetyl chloride 
• 103-82-2 phenylacetic acid 
• 4156-16-5 2-ethyl-5-phenylisoxazolium-3'-sulphonate 
• 914771-42-9 methanol ethyl acetate 
• 27532-96-3 glycine tert-butyl ester hydrochloride 
• 56-85-9 GLUTAMINE 
• 77658-84-5 N-(2,6-dioxopiperidin-3-yl)-2-phenylacetamide 
• 101-41-7 benzeneacetic acid methyl ester 

Downstream Products

• 103-82-2 phenylacetic acid 
• 6893-26-1 D-Glutamic acid 

Relevant articles and documents

Preparation of D-amino acids by enzymatic kinetic resolution using a mutant of penicillin-G acylase from E. coli

We have demonstrated for the first time that d-glutamine (d-Gln) and d-glutamic acid (d-Glu) can be efficiently obtained in high ee (97% and 90%, respectively) by enzymatic kinetic resolution of d,l-Gln and d,l-Glu. This was achieved by enantioselective conversion of the l-enantiomers to their N-phenylacetyl derivatives in aqueous solution, using a mutant of penicillin-G acylase (PGA) from E. coli and phenylacetic acid methylester as the acyl donor. Kinetic modeling studies suggest that the high ee values obtained are both due to a strong enantiopreference for the l-amino acid in the deacylation step of the covalent enzyme intermediate, as well as to completeness of conversion that is transiently obtained as a result of the distinct preference of the mutant PGA for phenylacetic acid methylester over the N-phenylacetyl-l-amino acid product. For the other amino acids tested (Asn, Asp, and Ser), the highest ee values that were obtained for the remaining d-enantiomer are moderate (50-80%) because of lower enantioselectivity in the enzyme deacylation step and due to less complete conversion of the l-amino acid caused by competition for the active site between the acyl donor and the N-phenylacetyl-l-amino acid that is produced. The results demonstrate that the mutated PGA has great potential for the production of optically active D-amino acids by kinetic resolution.

Phenylacetylglutamine (PAG) analytical test

The present invention is directed to a fluorescence polarization immunoassay for determining the phenylacetylglutamine (PAG) content in body fluids, to the various components needed for preparing and carrying out such an assay, and to the methods of making these components. Specifically, tracers, immunogens and antibodies are disclosed, as well as methods for preparing them. The assay is conducted by measuring the degree of polarization of plane polarized light that has been passed through a solution continuing sample, antiserum and tracer.