74069-74-2

Basic information

• Product Name: (R)-2-Nonanamine
• Synonyms: (R)-(-)-2-AMINONONANE;(R)-2-NONYLAMINE;(S)-(+)-2-AMINONONANE;(S)-2-NONYLAMINE;(2R)-Nonylamine;(R)-1-Methyloctylamine;(R)-(-)-2-AMINONONANE: CHIPROS 99%, EE 98%;(R)-(-)-2-Aminononane, ChiPros 99+%, ee 98+%
• CAS NO: 74069-74-2
• Molecular Formula: C₉H₂₁N
• Molecular Weight: 143.27
• EINECS: -0
• Mol File: 74069-74-2.mol
• Article Data: 4

Chemical Properties

• Melting Point: <-20°C
• Boiling Point: 73°C 19mm
• Flash Point: 71°C
• Appearance: /
• Density: 0,782 g/cm3
• Vapor Pressure: 0.526mmHg at 25°C
• Refractive Index: 1.4271
• Sensitive: Air Sensitive
• CAS DataBase Reference: (R)-2-Nonanamine(CAS DataBase Reference)
• NIST Chemistry Reference: (R)-2-Nonanamine(74069-74-2)
• EPA Substance Registry System: (R)-2-Nonanamine(74069-74-2)

Safety Data

• Hazard Codes: C,N
• Statements: 34-50/53-35-20/21/22
• Safety Statements: 26-36/37/39-45-61
• RIDADR: 2735
• WGK Germany: 3
• HazardClass: 8
• PackingGroup: II
• Hazardous Substances Data: 74069-74-2(Hazardous Substances Data)

Usage

General Description

"(R)-2-Nonanamine" is a chemical compound with the molecular formula C9H19N. Also known as (R)-(+)-2-Amino nonane, it is a chiral amine that consists of a nine-carbon chain with a primary amine group at the second carbon. (R)-2-Nonanamine is commonly used as a building block in the synthesis of pharmaceuticals, agrochemicals, and other organic compounds. It is also a potential target for research in the development of new drugs and materials. Additionally, (R)-2-Nonanamine has been studied for its role in certain biological processes and its potential applications in various industries.

InChI:InChI=1/C9H21N/c1-3-4-5-6-7-8-9(2)10/h9H,3-8,10H2,1-2H3/t9-/m1/s1

Upstream product

• 869278-88-6 (S)-(+)-2-aminononane 
• 5329-79-3 (R)‐2‐aminohexane 
• 821-55-6 2-Nonanone 

Downstream Products

• 821-55-6 2-Nonanone 
• 869278-88-6 (S)-(+)-2-aminononane 
• 5329-79-3 (R)‐2‐aminohexane 

Relevant articles and documents

Separate Sets of Mutations Enhance Activity and Substrate Scope of Amine Dehydrogenase

Mutations were introduced into the leucine amine dehydrogenase (L-AmDH) derived from G. stearothermophilus leucine dehydrogenase (LeuDH) with the goals of increased activity and expanded substrate acceptance. A triple variant (L-AmDH-TV) including D32A, F101S, and C290V showed an average of 2.5-fold higher activity toward aliphatic ketones and an 8.0 °C increase in melting temperature. L-AmDH-TV did not show significant changes in relative activity for different substrates. In contrast, L39A, L39G, A112G, and T133G in varied combinations added to L-AmDH-TV changed the shape of the substrate binding pocket. L-AmDH-TV was not active on ketones larger than 2-hexanone. L39A and L39G enabled activity for straight-chain ketones as large as 2-decanone and in combination with A112G enabled activity toward longer branched ketones including 5-methyl-2-octanone.

Enzymatic asymmetric synthesis of enantiomerically pure aliphatic, aromatic and arylaliphatic amines with (R)-selective amine transaminases

Seven (R)-selective amine transaminases (R-ATAs) recently discovered by an in silico-based approach in sequence databases were produced recombinantly in Escherichia coli and subjected to partial purification by ammonium sulfate precipitation. A range of additives and various buffers were investigated to identify best conditions to ensure good storage stability and stable activity during biocatalysis. All enzymes show pH optima between pH 7.5-9. These R-ATAs were then applied in the asymmetric synthesis of twelve aliphatic, aromatic and arylaliphatic (R)-amines starting from the corresponding prochiral ketones using a lactate dehydrogenase/glucose dehydrogenase system to shift the equilibrium. For all ketones, at least one enzyme was found that allows complete conversion to the corresponding chiral amine having excellent optical purities >99% ee. Variations in substrate profiles are also discussed based on the phylogenetic relationships between the seven R-ATAs. Thus, we have identified a versatile toolbox of (R)-amine transaminases showing remarkable properties for application in biocatalysis. Copyright