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Glycine, N-[N-[(phenylmethoxy)carbonyl]-L-tyrosyl]- is a complex organic compound that combines two amino acids, glycine and L-tyrosine, through a peptide bond. The L-tyrosine is modified with a phenylmethoxycarbonyl group, which is an ester derived from phenylmethanol and carbonic acid. Glycine, N-[N-[(phenylmethoxy)carbonyl]-L-tyrosyl]- is of interest in the field of organic chemistry and may have potential applications in the synthesis of pharmaceuticals or as a building block for more complex molecules. Its structure and properties make it a valuable component in the development of new compounds with specific biological activities.

2541-27-7

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2541-27-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 2541-27-7 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,5,4 and 1 respectively; the second part has 2 digits, 2 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 2541-27:
(6*2)+(5*5)+(4*4)+(3*1)+(2*2)+(1*7)=67
67 % 10 = 7
So 2541-27-7 is a valid CAS Registry Number.

2541-27-7SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 14, 2017

Revision Date: Aug 14, 2017

1.Identification

1.1 GHS Product identifier

Product name 2-[[(2S)-3-(4-hydroxyphenyl)-2-(phenylmethoxycarbonylamino)propanoyl]amino]acetic acid

1.2 Other means of identification

Product number -
Other names -

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

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More Details:2541-27-7 SDS

2541-27-7Relevant academic research and scientific papers

Synthesis of a precursor of bioactive pentapeptide OGP-(10-14) and the fragment of enkephalin catalyzed by MCM-22 immobilized or free proteases in organic solvents

Liu, Ping,Ye, Yun-Hua,Tian, Gui-Ling,Lee, Kin-Sing,Wong, Man-Sau,Lo, Wai-Hung

, p. 726 - 732 (2007/10/03)

Full enzymatic synthesis of a precursor of osteogenic growth peptide fragment (10-14), Z-Tyr-Gly-Phe-Gly-Gly-OEt, was accomplished using immobilized proteases on molecular sieve MCM-22 by adsorption as catalyst via 3+2 synthetic route for the first rime. The reuse time of immobilized enzyme was dependent on concrete reaction system. Compared with free enzyme, the reaction rate catalyzed by immobilized enzyme was remarkably enhanced and its synthetic yield was also increased in most cases. The effects of water content and the added amount of Et3N on synthesis of fragments of bioactive peptides including OGP-(10-14) and enkephalin by immobilized enzymes were different from free enzyme.

Antibody catalyzed modification of amino acids. Efficient hydrolysis of tyrosine benzoate

Benedetti,Berti,Colombatti,Flego,Gardossi,Linda,Peressini

, p. 715 - 716 (2007/10/03)

Esterase antibody 522c2, the first example of a catalytic antibody specifically programmed to control the reactivity of functional groups on the side chain of tyrosine, accelerates the hydrolysis of benzoate esters of L-tyrosine and tyrosine-containing dipeptides by a factor of 104 and is moderately active against other benzoate esters.

Synthesis and analysis of Leu-enkephalin analogues containing reverse turn peptidomimetics

Claridge, Timothy D. W.,Hulme, Christopher,Kelly, Richard J.,Lee, Victor,Nash, Ian A.,Schofield, Christopher J.

, p. 485 - 490 (2007/10/03)

The synthesis and 1H n.m.r. analysis of peptidomimetics of Leu-enkephalin containing bicyclic lactams is described.

Carbohydrate Protease Conjugates: Stabilized Proteases for Peptide Synthesis

Wartchow, Charles A.,Wang, Peng,Bednarski, Mark D.,Callstrom, Matthew R.

, p. 2216 - 2226 (2007/10/02)

The synthesis of oligopeptides using stable carbohydrate protease conjugates (CPCs) was examined in acetonitrile solvent systems.CPC was used for the preparation of peptides containing histidine, phenylalanine, tyrosine, and tryptophan in the P1 position in 60-93percent yield.The CPC was used to synthesize peptides containing both hydrophilic and hydrophobic amino acids.The P2 specificity of papain for aromatic residues was utilized for the 2 + 3 coupling of Z-Tyr-Gly-OMe to H2N-Gly-Phe-Leu-OH to generate the leucine enkephalin derivative in 79percent yield.Although papain is nonspecific for the hydrolysis of N-benzyloxycarbonyl amino acid methyl esters in aqueous solution, the rates of synthesis for these derivatives with nucleophile leucine tert-butyl ester differed by nearly 2 orders of magnitude.CPC was used to prepare the aspartame precursor Z-Asp-Phe-OMe in 90percent yield.The increased stability of CPCs prepared from periodate-modified poly(2-methacrylamido-2-deoxy-D-glucose), poly(2-methacrylamido-2-deoxy-D-galactose), and poly(5-methacrylamido-5-deoxy-D-ribose), carbohydrate materials designed to increase the aldehyde concentration in aqueous solution, suggests that the stability of CPCs is directly related to the aldehyde concentration of the carbohydrate material.Periodate oxidation of poly(2-methacrylamido-2-deoxy-D-glucose) followed by covalent attachment to α-chymotrypsin gave a CPC with catalytic activity in potassium phosphate buffer at 90 deg C for 2 h.

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