73731-37-0

Basic information

• Product Name: 2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-hydroxy-butanoic acid
• Synonyms: FMOC-L-THREONINE extrapure;N-(9-Fluorenylmethoxycarbonyl)-L-threonine ,99%;N-alpha-(9-fluorenylmethyloxycarbonylamino)-3-hydroxybutanoic acid;Fmoc-L-threonine ,99%;Fmoc-L-Threonine monohydrate ,99%;Fmoc-Threonine-OH;2-(9H-Fluoren-9-ylMethoxycarbony-laMino)-3-;FMoc-Thr-OH·H2O FMoc-L-threonine Monohydrate
• CAS NO: 73731-37-0
• Molecular Formula: C₁₉H₁₉NO₅
• Molecular Weight: 341.36
• EINECS: 1533716-785-6
• Product Categories: Threonine [Thr, T];Fmoc-Amino Acids and Derivatives;Amino Acids (N-Protected);Biochemistry;Fmoc-Amino Acids;Fmoc-Amino acid series;Amino Acid Derivatives;Amino Acids
• Mol File: 73731-37-0.mol
• Article Data: 24

Chemical Properties

• Melting Point: 115°C (dec.)
• Boiling Point: 596.5 °C at 760 mmHg
• Flash Point: 314.6 °C
• Appearance: /
• Density: 1.327 g/cm³
• Vapor Pressure: 4.45E-15mmHg at 25°C
• Refractive Index: -15.5 ° (C=1, DMF)
• Storage Temp.: 2-8°C
• Solubility: soluble in Methanol
• PKA: 3.49±0.10(Predicted)
• BRN: 4300093
• CAS DataBase Reference: 2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-hydroxy-butanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-hydroxy-butanoic acid(73731-37-0)
• EPA Substance Registry System: 2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-hydroxy-butanoic acid(73731-37-0)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 22-24/25-26
• WGK Germany: 3
• Hazardous Substances Data: 73731-37-0(Hazardous Substances Data)

Usage

Description

2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-hydroxy-butanoic acid, also known as N-Fmoc-L-threonine, is an N-Fmoc-protected form of L-threonine, an essential amino acid. It is commonly used as a feed and food additive and is produced in mass quantities by mutant Escherichia coli strains for research and food nutrition purposes. L-threonine can be naturally found in fish and poultry and is incorporated in some important proteins in the human body, such as hemoglobin and insulin.

Uses

Used in Pharmaceutical Industry:
N-Fmoc-L-threonine is used as a building block for the synthesis of peptides and proteins in the pharmaceutical industry. Its Fmoc protection group allows for selective deprotection and coupling reactions, facilitating the assembly of complex peptide structures.
Used in Food and Nutrition Industry:
N-Fmoc-L-threonine is used as a feed and food additive to enhance the nutritional value of products. As an essential amino acid, it plays a crucial role in the growth and maintenance of tissues and contributes to the overall protein synthesis in the body.
Used in Research Applications:
N-Fmoc-L-threonine is used as a research tool for studying protein synthesis, structure, and function. Its Fmoc protection group allows for controlled synthesis of peptides and proteins, making it a valuable reagent in biochemical and biophysical research.

InChI:InChI=1/C19H19NO5/c1-11(21)17(18(22)23)20-19(24)25-10-16-14-8-4-2-6-12(14)13-7-3-5-9-15(13)16/h2-9,11,16-17,21H,10H2,1H3,(H,20,24)(H,22,23)/t11-,17+/m1/s1

Upstream product

• 72-19-5 L-threonine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 88744-04-1 (9-fluorenyl)methyl pentafluorophenyl carbonate 
• 133180-01-5 Fmoc-O-trityl-l-threonine 
• 176380-53-3 (2R,3R)-2-(9H-fluoren-9-ylmethoxycarbonylamino)butane-1,3-diol 
• 377082-52-5 (2R,3R)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-1-O-(tert-butyldimethylsilyl)butane-1,3-diol 
• 24324-17-2 9-Fluorenylmethanol 
• 82911-72-6 dicyclohexylamine salt of N-hydroxysuccinimide 
• 101-83-7 N-cyclohexyl-cyclohexanamine 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 71989-35-0 Fmoc-Thr(tBu)-OH 
• 918531-00-7 N-(9H-9-fluoren-9-yl)methoxycarbonyl-O-tetrahydro-2H-pyran-2-yl-L-threonine 
• 89024-98-6 N-α-(9-fluorenylmethyloxycarbonyl)-L-threonine methyl ester 

Downstream Products

• 102410-67-3 Fmoc-Thr-D-Abu-Pro-OBu^t 
• 169219-08-3 N^α-(9-fluorenylmethoxycarbonyl)-3-O-(2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl)-L-threonine 
• 150672-50-7 (2S,3R)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-hydroxy-butyric acid 3-methyl-oxetan-3-ylmethyl ester 

Relevant articles and documents

Novel chiral stationary phases based on 3,5-dimethyl phenylcarbamoylated β-cyclodextrin combining cinchona alkaloid moiety

Novel chiral selectors based on 3,5-dimethyl phenylcarbamoylated β-cyclodextrin connecting quinine (QN) or quinidine (QD) moiety were synthesized and immobilized on silica gel. Their chromatographic performances were investigated by comparing to the 3,5-dimethyl phenylcarbamoylated β-cyclodextrin (β-CD) chiral stationary phase (CSP) and 9-O-(tert-butylcarbamoyl)-QN-based CSP (QN-AX). Fmoc-protected amino acids, chiral drug cloprostenol (which has been successfully employed in veterinary medicine), and neutral chiral analytes were evaluated on CSPs, and the results showed that the novel CSPs characterized as both enantioseparation capabilities of CD-based CSP and QN/QD-based CSPs have broader application range than β-CD-based CSP or QN/QD-based CSPs. It was found that QN/QD moieties play a dominant role in the overall enantioseparation process of Fmoc-amino acids accompanied by the synergistic effect of β-CD moiety, which lead to the different enantioseparation of β-CD-QN-based CSP and β-CD-QD-based CSP. Furthermore, new CSPs retain extraordinary enantioseparation of cyclodextrin-based CSP for some neutral analytes on normal phase and even exhibit better enantioseparation than the corresponding β-CD-based CSP for certain samples.

A Threonine-Forming Oxazetidine Amino Acid for the Chemical Synthesis of Proteins through KAHA Ligation

α-Ketoacid-hydroxylamine (KAHA) ligation allows the coupling of unprotected peptide segments through the chemoselective formation of an amide bond. Currently, the most widely used variant employs a 5-membered cyclic hydroxylamine that forms a homoserine ester as the primary ligation product. In order to directly form amide-linked threonine residues at the ligation site, we prepared a new 4-membered cyclic hydroxylamine building block. This monomer was applied to the synthesis of wild-type ubiquitin-conjugating enzyme UbcH5a (146 residues) and Titin protein domain TI I27 (89 residues). Both the resulting UbcH5a and the variant with two homoserine residues showed identical activity to a recombinant variant in a ubiquitination assay.

Fmoc-OPhth, the reagent of Fmoc protection

Fmoc-OSu has been widely used for Fmoc protection of amino groups, especially amino acids, in solid phase peptide synthesis. However, it has been recognized that Fmoc-βAla-OH is formed as a by-product via the Lossen rearrangement during the reaction. Since we reconfirmed the formation of Fmoc-βAla-OH during the preparation of Fmoc-AA-OH by Fmoc-OSu, Fmoc-OPhth was designed and synthesized as a new Fmoc reagent to avoid the formation of Fmoc-βAla-OH. Furthermore, Fmoc protection by Fmoc-OPhth and Fmoc-SPPS were evaluated. The various Fmoc-amino acids prepared by Fmoc-OPhth were carried out in good yields and these are applicable in Fmoc-SPPS.