121786-28-5

Basic information

• Product Name: (4E)-2-amino-5-phenylpent-4-enoic acid
• Synonyms: (4E)-2-amino-5-phenylpent-4-enoic acid
• CAS NO: 121786-28-5
• Molecular Formula: C₁₁H₁₃NO₂
• Molecular Weight: 191.23
• Mol File: 121786-28-5.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• CAS DataBase Reference: (4E)-2-amino-5-phenylpent-4-enoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: (4E)-2-amino-5-phenylpent-4-enoic acid(121786-28-5)
• EPA Substance Registry System: (4E)-2-amino-5-phenylpent-4-enoic acid(121786-28-5)

Safety Data

• Hazardous Substances Data: 121786-28-5(Hazardous Substances Data)

Usage

Description

(4E)-2-amino-5-phenylpent-4-enoic acid, also known as t-2-amino-5-phenyl-4-pentenoic acid, is a chemical compound with the molecular formula C11H13NO2. It is an amino acid derivative that contains an amino group and a phenyl group attached to a pent-4-enoic acid functional group. (4E)-2-amino-5-phenylpent-4-enoic acid is not a naturally occurring amino acid and is not commonly found in biological systems. It may be used as a building block in organic synthesis or as a reagent in chemical reactions. Its specific properties and potential applications in science and industry may vary depending on the context and intended use.

Uses

Used in Organic Synthesis:
(4E)-2-amino-5-phenylpent-4-enoic acid is used as a building block for the synthesis of various organic compounds. Its unique structure, which includes an amino group, a phenyl group, and a pent-4-enoic acid functional group, allows it to be a versatile component in the creation of complex molecules for a wide range of applications.
Used in Chemical Reactions:
As a reagent, (4E)-2-amino-5-phenylpent-4-enoic acid can be employed in various chemical reactions to facilitate the formation of desired products. Its presence may help in the synthesis of pharmaceuticals, agrochemicals, or other specialty chemicals, depending on the specific reaction conditions and the goals of the synthesis process.
Used in Research and Development:
(4E)-2-amino-5-phenylpent-4-enoic acid may also be utilized in research and development settings to explore its properties and potential applications. Scientists and chemists can investigate its reactivity, stability, and interactions with other compounds, which could lead to the discovery of new uses or improvements in existing processes.

Upstream product

• 101583-20-4 cis-cinnamyl-formylamino-malonic acid diethyl ester 
• 101585-55-1 formylamino-(3-phenyl-prop-2-ynyl)-malonic acid diethyl ester 
• 1794-48-5 1-bromo-3-phenylprop-2-yne 
• 52161-76-9 (+/-)-2-amino-5c-phenyl-pent-4-enoic acid 
• 101583-20-4 trans-cinnamyl-formylamino-malonic acid diethyl ester 
• 4746-62-7 2-amino-2-hydroxyacetic acid 
• 147609-46-9 2-(2E)-(3-phenyl-2-propen-1-yl)-4,4,5,5-tetramethyl-1,3,2-dioxaborolane 
• 21087-29-6 trans-3-phenylprop-2-enyl chloride 
• 109838-85-9 (2R)-2,5-dihydro-2-isopropyl-3,6-dimethoxypyrazine 
• 4392-24-9 Cinnamyl bromide 
• 4392-24-9 3-bromo-1-phenyl-1-propenyl bromide 
• 101782-54-1 Acetamino-cinnamyl-malonsaeure-diethylester 
• 108246-15-7 (+/-)-4-Acetamino-1-phenyl-penten-⁽¹⁾-saeure-⁽⁵⁾ 

Downstream Products

• 121786-28-5 rac-(E)-2-amino-5-phenylpent-4-enoic acid 
• 28010-12-0 5-phenylpenta-2,4-dienoic acid 
• 267650-37-3 (R,E)-2-amino-5-phenylpent-4-enoic acid 
• 52161-76-9 (E,2S)-2-amino-5-phenyl-pent-4-enoic acid 

Relevant articles and documents

Expanding the substrate scope of phenylalanine ammonia-lyase from: Petroselinum crispum towards styrylalanines

This study focuses on the expansion of the substrate scope of phenylalanine ammonia-lyase from Petroselinum crispum (PcPAL) towards the l-enantiomers of racemic styrylalanines rac-1a-d-which are less studied and synthetically challenging unnatural amino acids-by reshaping the aromatic binding pocket of the active site of PcPAL by point mutations. Ammonia elimination from l-styrylalanine (l-1a) catalyzed by non-mutated PcPAL (wt-PcPAL) took place with a 777-fold lower kcat/KM value than the deamination of the natural substrate, l-Phe. Computer modeling of the reactions catalyzed by wt-PcPAL indicated an unproductive and two major catalytically active conformations and detrimental interactions between the aromatic moiety of l-styrylalanine, l-1a, and the phenyl ring of the residue F137 in the aromatic binding region of the active site. Replacing the residue F137 by smaller hydrophobic residues resulted in a small mutant library (F137X-PcPAL, X being V, A, and G), from which F137V-PcPAL could transform l-styrylalanine with comparable activity to that of the wt-PcPAL with l-Phe. Furthermore, F137V-PcPAL showed superior catalytic efficiency in the ammonia elimination reaction of several racemic styrylalanine derivatives (rac-1a-d) providing access to d-1a-d by kinetic resolution, even though the d-enantiomers proved to be reversible inhibitors. The enhanced catalytic efficiency of F137V-PcPAL towards racemic styrylalanines rac-1a-d could be rationalized by molecular modeling, indicating the more relaxed enzyme-substrate complexes and the promotion of conformations with higher catalytic activities as the main reasons. Unfortunately, ammonia addition onto the corresponding styrylacrylates 2a-d failed with both wt-PcPAL and F137V-PcPAL. The low equilibrium constant of the ammonia addition, the poor ligand binding affinities of 2a-d, and the non-productive binding states of the unsaturated ligands 2a-d within the active sites of either wt-PcPAL or F137V-PcPAL-as indicated by molecular modeling-might be responsible for the inactivity of the PcPAL variants in the reverse reaction. Modeling predicted that the F137V mutation is beneficial for the KRs of 4-fluoro-, 4-cyano- and 4-bromostyrylalanines, but non-effective for the KR process of 4-trifluoromethylstyrylalanine.

Single chain peptide compounds having hemoregulatory activity

There is disclosed single chain peptide compounds, substituted at a Cα-atom of a non-terminal amino acid by a group--A which is defined in claim 1. The native α-side chain of the Cα atom bonded group to group --A absent. The peptide derivatives according