28047-15-6

Usage

Uses

Used in Medical and Biotechnology Industry:
PHENYLAC-GLN-OH is used as a biomarker for metabolic age, providing valuable insights into the aging process and its relationship with metabolic health. This application aids in the development of targeted therapies and interventions to improve overall health and longevity.
Used in Research and Diagnostics:
As a biomarker for metabolic age, PHENYLAC-GLN-OH is also utilized in research and diagnostics to study the effects of various factors on aging and metabolism. This helps in understanding the underlying mechanisms and developing strategies to counteract age-related metabolic changes.
Chemical Properties:
PHENYLAC-GLN-OH is characterized by its white solid appearance, which is indicative of its stable and consistent chemical properties. These properties make it suitable for use in various applications across different industries.

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 
• 77658-84-5 N-(2,6-dioxopiperidin-3-yl)-2-phenylacetamide 
• 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 
• 101-41-7 benzeneacetic acid methyl ester 

Downstream Products

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

Relevant academic research and scientific papers

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.

3-[(Phenylacetyl)amino]-2,6-piperidinedione hydrolysis studies with improved synthesis and characterization of hydrolysates

In an attempt to clarify ambiguities in earlier reports on the preclinical chemistry of Antineoplaston A10 (3-[(phenylacetyl)amino]-2,6- piperidinedione; PAP), we detail herein hydrolysis studies with improved synthesis and characterization of PAP hydrolysis products, (phenylacetyl)- glutamine (PAG), (phenylacetyl)isoglutamine (PAIG), and (phenylacetyl)- glutamic acid (PAGA). Flash chromatography proved superior to extraction in the isolation of synthetic standards and hydrolysates. Synthesis of PAIG directly from commercial isoglutamine showed consistently better yields than the previously reported method. The 1H and 13C NMR and HPLC-MS data from the synthesized standards matched the data from the isolated PAP hydrolysates formed under acid and alkaline degradation conditions. Multiple quantum coherence NMR methods (HMQC and HMBC) and HPLC-MS-MS methods were applied to provide unambiguous structural assignments for key isomers PAG and PAIG. Previous PAP hydrolysis studies are shown to be reproducible, and the structures of hydrolysis products are elucidated in detail.

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.