10325-17-4

Basic information

• Product Name: (D,L)-2-AMINO-HEPT-6-ENOIC ACID
• Synonyms: (D,L)-2-AMINO-HEPT-6-ENOIC ACID;2-amino-6-Heptenoic acid
• CAS NO: 10325-17-4
• Molecular Formula: C7H13NO2
• Molecular Weight: 143.18
• Mol File: 10325-17-4.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• CAS DataBase Reference: (D,L)-2-AMINO-HEPT-6-ENOIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: (D,L)-2-AMINO-HEPT-6-ENOIC ACID(10325-17-4)
• EPA Substance Registry System: (D,L)-2-AMINO-HEPT-6-ENOIC ACID(10325-17-4)

Safety Data

• Hazardous Substances Data: 10325-17-4(Hazardous Substances Data)

Usage

General Description

(D,L)-2-AMINO-HEPT-6-ENOIC ACID is a chemical compound with the molecular formula C7H13NO2. It is an amino acid, specifically an unsaturated amino acid, that plays an important role in the biosynthesis of a variety of natural products. (D,L)-2-AMINO-HEPT-6-ENOIC ACID is also known as 2-amino-7-en-6-heptenoic acid and is commonly found in certain bacteria and fungi. It is involved in the synthesis of secondary metabolites and has also been studied for potential medicinal applications. Overall, (D,L)-2-AMINO-HEPT-6-ENOIC ACID is an important building block in the production of various natural compounds and has potential applications in the pharmaceutical and biotechnology industries.

Upstream product

• 31918-33-9 2-Oximino-6-heptensaeureethylester 
• 1119-51-3 bromopentene 
• 1906-96-3 diethyl (4-pentenyl)malonate 
• 56548-08-4 Pent-4-enyl-cyan-acetamino-essigsaeure-aethylester 

Relevant articles and documents

Synthesis of unsaturated alpha-amino-acids.

-

A Biocatalytic Route to Enantiomerically Pure Unsaturated α-H-α-Amino Acids

A set of both enantiomeric forms of non-proteinogenic, unsaturated α-H-α-amino acids was efficiently synthesized using a biocatalytic pathway. This route involved the straightforward synthesis of the required unsaturated amino acid amides, followed by resolution with an aminopeptidase present in Pseudomonas putida ATCC 12633 and/or a genetically modified organism, leading to the (S)-acids and (R)-amides. Undesired amino acid racemase activity was identified in the wild-type strain, which was absent in the newly developed organism. The (R)-amides were hydrolyzed under mild conditions using an amidase present in whole cells from Rhodococcus erythropolis NCIMB 11540 to the (R)-acids. The viability of this procedure was demonstrated with the multi-gram synthesis of a variety of unsaturated amino acids in excellent enantiopurity.