90989-12-1

Basic information

• Product Name: (2S)-2-AMINO-5-HEXENOIC ACID
• Synonyms: (2S)-2-AMINO-5-HEXENOIC ACID;(S)- 2-(3'-butenyl) glycine;(S)-2-AMino-5-hexenoic acid;(S)-2-Aminohex-5-enoic acid
• CAS NO: 90989-12-1
• Molecular Formula: C₆H₁₁NO₂
• Molecular Weight: 129.16
• Product Categories: amino acids
• Mol File: 90989-12-1.mol
• Article Data: 14

Chemical Properties

• Melting Point: >270 °C
• Boiling Point: 242.0±28.0 °C(Predicted)
• Appearance: /
• Density: 1.064±0.06 g/cm3(Predicted)
• Storage Temp.: Keep in dark place,Inert atmosphere,Room temperature
• PKA: 2.31±0.10(Predicted)
• CAS DataBase Reference: (2S)-2-AMINO-5-HEXENOIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: (2S)-2-AMINO-5-HEXENOIC ACID(90989-12-1)
• EPA Substance Registry System: (2S)-2-AMINO-5-HEXENOIC ACID(90989-12-1)

Safety Data

• Hazardous Substances Data: 90989-12-1(Hazardous Substances Data)

Usage

General Description

(2S)-2-AMINO-5-HEXENOIC ACID is a chemical compound with the molecular formula C6H11NO2. It is an amino acid, specifically a derivative of glutamic acid, and is commonly known as norleucine. It contains a hexenoic acid side chain and a primary amino group, and exists as a white crystalline solid at room temperature. (2S)-2-AMINO-5-HEXENOIC ACID is an important intermediate in the biosynthesis of certain proteins, and is also used in the production of various pharmaceuticals and biochemical research. Additionally, it has potential applications in the food industry as a flavor enhancer. Overall, (2S)-2-AMINO-5-HEXENOIC ACID plays a significant role in various biological and industrial processes.

Upstream product

• 141943-64-8 (±)-2-acetamidohex-5-enoic acid 
• 161633-97-2 (R)-4-Methyl-2-((4S,5R)-2-oxo-4,5-diphenyl-oxazolidin-3-yl)-pent-4-enoic acid benzyl ester 
• 5162-44-7 1-bromo-4-butene 
• 90877-70-6 ethyl 2-acetamido-2-cyanoacetate 
• 188194-81-2 2-amino-5-hexenoic acid amide 
• 122471-00-5 acetylamino-3-butenyl-propanedioic acid diethyl ester 
• 1095239-02-3 (R,R)-pseudoephedrine (S)-2-amino-5-hexenoic amide 
• 226985-05-3 (S)-(-)-1-tert-butyl-2--5-hexenoate 
• 410098-01-0 (2S)-2-aminohex-5-enoic acid methyl ester 

Downstream Products

• 141362-49-4 phenylmethyl (S)-2-amino-5-hexenoate 
• 851909-08-5 (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)hex-5-enoic acid 
• 148696-56-4 (2S,5S,7aR)-2-Benzyl-3-oxo-hexahydro-pyrrolo[1,2-a]imidazole-1,5-dicarboxylic acid 1-benzyl ester 
• 148696-57-5 (2S,5S,7aR)-2-Benzyl-5-isobutylcarbamoyl-3-oxo-hexahydro-pyrrolo[1,2-a]imidazole-1-carboxylic acid benzyl ester 
• 148696-50-8 (S)-2-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-hex-5-enoic acid benzyl ester 
• 148696-49-5 (2S,5S,7aR)-2-Benzyl-3-oxo-hexahydro-pyrrolo[1,2-a]imidazole-1,5-dicarboxylic acid dibenzyl ester 
• 148696-51-9 (S)-2-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-5-oxo-pentanoic acid benzyl ester 
• 141943-65-9 benzyl (S)-2-(p-tolylsulfonylamino)hex-5-enone 
• 208522-13-8 (S)-2-N-(tert-butoxycarbonyl)-2-amino-5-hexenoic acid 
• 1195070-20-2 Fmoc-L-Asn(Trt)-L-Hag-OH 
• 155905-76-3 (2S)-1-(tert-butoxycarbonyl)-2-azepanecarboxylic acid 

Relevant articles and documents

Macrocyclic BACE1 inhibitors with hydrophobic cross-linked structures: Optimization of ring size and ring structure

Based on the X-ray crystallography of recombinant BACE1 and a hydroxyethylamine-type peptidic inhibitor, we introduced a cross-linked structure between the P1 and P3 side chains of the inhibitor to enhance its inhibitory activity. The P1 and P3 fragments bearing terminal alkenes were synthesized, and a ring-closing metathesis of these alkenes was used to construct the cross-linked structure. Evaluation of ring size using P1 and P3 fragments with various side chain lengths revealed that 13-membered rings were optimal, although their activity was reduced compared to that of the parent compound. Furthermore, the optimal ring structure was found to be a macrocycle with a dimethyl branched substituent at the P3 β-position, which was approximately 100-fold more active than the non-substituted macrocycle. In addition, the introduction of a 4-carboxymethylphenyl group at the P1′ position further improved the activity.

Influence of Sulfoxide Group Placement on Polypeptide Conformational Stability

The synthesis of a homologous series containing five new nonionic sulfoxide containing polypeptides was described. Sulfoxide groups bestowed water solubility for all homologues, which allowed their use as a model for study of helix-coil transitions in water while avoiding contributions from charged groups or phase separation. Polypeptides were found to adopt chain conformations in water that were dependent on distance of sulfoxides from chain backbones, overall side-chain lengths, and solvent. These results allow preparation of polypeptide segments with different chain conformations without changing chemical functionality for potential use in structural studies and functional applications.

Influence of α-methylation in constructing stapled peptides with olefin metathesis

Ring-closing metathesis is commonly utilized in peptide macro-cyclization. The influence of α-methylation of the amino acids bearing the olefin moieties has never been systematically studied. In this report, controlled reactions unambiguously indicate that α-methylation at the N-terminus of the metathesis sites is crucial for this reaction to occur. Also, we first elucidated that the E-isomers of stapled peptides are significantly more helical than the Z-isomers.