27796-49-2

Basic information

• Product Name: N-(2-Methoxybenzoyl)glycine methyl ester
• Synonyms: Methyl o-methoxyhippurate;N-(2-Methoxybenzoyl)glycine methyl ester;o-Methoxyhippuric acid methyl
• CAS NO: 27796-49-2
• Molecular Formula: C₁₁H₁₃NO₄
• Molecular Weight: 223.23
• Mol File: 27796-49-2.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 386°C at 760 mmHg
• Flash Point: 187.2°C
• Appearance: /
• Density: 1.173g/cm³
• Vapor Pressure: 3.66E-06mmHg at 25°C
• Refractive Index: 1.517
• CAS DataBase Reference: N-(2-Methoxybenzoyl)glycine methyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: N-(2-Methoxybenzoyl)glycine methyl ester(27796-49-2)
• EPA Substance Registry System: N-(2-Methoxybenzoyl)glycine methyl ester(27796-49-2)

Safety Data

• Hazardous Substances Data: 27796-49-2(Hazardous Substances Data)

Usage

InChI:InChI=1/C11H13NO4/c1-15-9-6-4-3-5-8(9)11(14)12-7-10(13)16-2/h3-6H,7H2,1-2H3,(H,12,14)

Upstream product

• 529-28-2 4-iodoanisol 
• 201230-82-2 carbon monoxide 
• 5680-79-5 glycine ethyl ester hydrochloride 
• 579-75-9 2-Methoxybenzoic acid 
• 616-34-2 methoxycarbonylmethylamine 

Downstream Products

• 487-54-7 Salicyluric acid 

Relevant articles and documents

Titanium-catalyzed stereoselective synthesis of spirooxindole oxazolines

A regio-and stereoselective cyclization between isatins and 5-methoxyoxazoles has been developed using catalytic titanium (IV) chloride (10 or 20 mol %) to afford spiro[3,3'-oxindoleoxazolines] in excellent yield (up to 99%) and diastereoselectivity (dr >

Substrate Specificity and Stoichiometry of Nα-Benzyloxycarbonyl Amino Acid Urethane Hydrolase from Streptococcus faecalis R ATCC 8043

The substrate specificity of a new enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase, was investigated.The enzyme hydrolyzed Nα-benzyloxycarbonyl-glycine and -alanine, and Nα-benzoyl-glycine and -alanine.Nα-benzyloxycarbonyl-glycine was hydrolyzed to give equimolar benzyl alcohol and glycine.Equimolar benzoic acid and glycine were produced from Nα-benzoyl-glycine by the enzyme reaction.The Km, k0, and k0/Km values were measured for several substrates.The k0 values varied widely with the amino acid residues.Nα-benzyloxycarbonyl-glycine and Nα-benzoyl-glycine produced relatively small changes in the Km values (0.36 ca. 0.10 mM) and the k0/Km values (99440 ca. 202000 M-1 sec-1).The rate of hydrolysis is significantly affected by electron-supplying substituents on the benzene ring.