2752-52-5

Basic information

• Product Name: N-(phenylacetyl)isoleucine
• CAS NO: 2752-52-5
• Molecular Formula: C₁₄H₁₉NO₃
• Molecular Weight: 249.3056
• Mol File: 2752-52-5.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 476.9°C at 760 mmHg
• Flash Point: 242.2°C
• Density: 1.119g/cm³
• Vapor Pressure: 6.67E-10mmHg at 25°C
• Refractive Index: 1.529
• CAS DataBase Reference: N-(phenylacetyl)isoleucine(CAS DataBase Reference)
• NIST Chemistry Reference: N-(phenylacetyl)isoleucine(2752-52-5)
• EPA Substance Registry System: N-(phenylacetyl)isoleucine(2752-52-5)

Safety Data

• Hazardous Substances Data: 2752-52-5(Hazardous Substances Data)

Upstream product

• 73-32-5 DL-isoleucine 
• 103-80-0 phenylacetyl chloride 
• 103-82-2 phenylacetic acid 
• 101-41-7 benzeneacetic acid methyl ester 
• 73-32-5 L-isoleucine 

Downstream Products

• 116912-14-2 N-(Phenylacetyl)-L-isoleucyl-L-alanin-allylester 
• 116912-14-2 PhAc-Ile-Ala-OAll 

Relevant articles and documents

Discovery, characterization and engineering of ligases for amide synthesis

Coronatine and related bacterial phytotoxins are mimics of the hormone jasmonyl-l-isoleucine (JA-Ile), which mediates physiologically important plant signalling pathways1–4. Coronatine-like phytotoxins disrupt these essential pathways and have potential in the development of safer, more selective herbicides. Although the biosynthesis of coronatine has been investigated previously, the nature of the enzyme that catalyses the crucial coupling of coronafacic acid to amino acids remains unknown1,2. Here we characterize a family of enzymes, coronafacic acid ligases (CfaLs), and resolve their structures. We found that CfaL can also produce JA-Ile, despite low similarity with the Jar1 enzyme that is responsible for ligation of JA and l-Ile in plants5. This suggests that Jar1 and CfaL evolved independently to catalyse similar reactions—Jar1 producing a compound essential for plant development4,5, and the bacterial ligases producing analogues toxic to plants. We further demonstrate how CfaL enzymes can be used to synthesize a diverse array of amides, obviating the need for protecting groups. Highly selective kinetic resolutions of racemic donor or acceptor substrates were achieved, affording homochiral products. We also used structure-guided mutagenesis to engineer improved CfaL variants. Together, these results show that CfaLs can deliver a wide range of amides for agrochemical, pharmaceutical and other applications.

AZAINDOLINE COMPOUNDS AS GRANZYME B INHIBITORS

Azaindoline compounds as granzyme B inhibitors, compositions that include the compounds, and methods for using the compounds. Methods for treating cutaneous scleroderma, epidermolysis bullosa, radiation dermatitis, alopecia areata, and discoid lupus erythematosus are provided.

Approaches to design non-covalent inhibitors for human granzyme B (hGrB)

A structure-based design campaign for non-covalent small molecule inhibitors of human granzyme B was carried out by means of a virtual screening strategy employing three constraints and probe site-mapping with FTMAP to identify ligand "hot spots". In addition, new scaffolds of diverse structures were subsequently explored with ROCS shape-based superposition methods, following by Glide SP docking, induced fit docking and analysis of QikProp molecular properties. Novel classes of moderately active small molecule blockers (≥25 μM IC50 values) from commercially available libraries were identified, and three novel scaffolds have been synthesized by multi-step procedures. Furthermore, we provide an example of a comprehensive structure-based drug discovery approach to non-covalent inhibitors that relies on the X-ray structure of a covalently bound ligand and suggest that the design path may be compromised by alternative and unknown binding poses. This journal is