32775-95-4

Basic information

• Product Name: (E)-3,5-hexadienoic acid
• Synonyms: (E)-3,5-hexadienoic acid
• CAS NO: 32775-95-4
• Molecular Weight: 112.128
• Mol File: 32775-95-4.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: (E)-3,5-hexadienoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: (E)-3,5-hexadienoic acid(32775-95-4)
• EPA Substance Registry System: (E)-3,5-hexadienoic acid(32775-95-4)

Safety Data

• Hazardous Substances Data: 32775-95-4(Hazardous Substances Data)

Upstream product

• 73670-87-8 (E)-hexa-3,5-dien-1-ol 
• 142252-83-3 C₆H₆O₂^(2-)*2Li⁽¹⁺⁾ 
• 98-86-2 acetophenone 
• 108-94-1 cyclohexanone 
• 54435-79-9 (E)-1,3-diphenyl-3-methyl-2-propen-1-one 
• 119-61-9 benzophenone 

Downstream Products

• 87785-65-7 p-nitrobenzyl 3,5-hexadienoate 
• 1413941-02-2 (3aS,4R,5R,5aS,8aS,8bS)-hexahydro-2,2,7,7-tetramethyl-5-{[(2E)-3-phenylprop-2-enoyl]oxy}benzo[1,2-d:3,4-d’]bis[1,3]dioxol-4-yl (3E)-hexa-3,5-dienoate 
• 1413941-05-5 (3aS,4R,5R,5aS,8aS,8bS)-5-{[(2E)-3-(4-bromophenyl)prop-2-enoyl]oxy}hexahydro-2,2,7,7-tetramethylbenzo[1,2-d:3,4-d']bis[1,3]dioxol-4-yl (3E)-hexa-3,5-dienoate 
• 3916-64-1 hepta-3,5-dien-2-one 
• 94291-57-3 (E)-hepta-4,6-dien-2-one 

Relevant articles and documents

Studies of acyl-CoA dehydrogenase catalyzed allylic isomerization: A one-base or two-base mechanism?

Acyl-CoA dehydrogenases are flavoproteins that catalyze the conversion of a fatty acyl thioester substrate to the corresponding α,β-enoyl-CoA product. It has been well established that a glutamate residue in the active site [e.g., E367 in short-chain acyl-CoA dehydrogenase (SCAD) of Megasphaera elsdenii] is responsible for the initial α-proton abstraction. Early studies have also shown that this class of enzymes is capable of catalyzing γ-H abstraction to afford the allylic isomerization between α,β- and β,γ-enone thioesters and/or inactivation by 2- or 3-acetylenic acyl-CoA derivatives. Although a dual role has been proposed for the glutamate residue in both α- and γ-deprotonation, the existence of a second active-site basic group to mediate the observed reactions occurring at γ-C remains a feasible mechanism. In an attempt to discern between these two possibilities, we have prepared a few oxirane-containing acyl-CoA derivatives aimed at trapping active-site bases in the vicinity of the α- and/or γ-C. It was found that 2,3-epoxybutyryl-CoA is a new class-selective irreversible inactivator against SCAD; however, the inability of other oxirane-containing probes to react with these enzymes prompted us to tackle this mechanistic problem by directly studying the role of Glu-367 in SCAD-catalyzed 1,3-isomerization. The effect of E367Q mutation on the proficiency of SCAD to mediate the γ-H exchange of crotonoyl-CoA was examined. The capabilities of the wild-type SCAD and its E367Q mutant to catalyze the γ-H abstraction during the inactivation by 2-butynoyl-CoA was also compared. The fact that the mutant protein fails to promote γ-H exchange/abstraction provides strong evidence supporting a one-base mechanism of this enzyme-catalyzed allylic isomerization. Since the catalysis of acyl-CoA dehydrogenases is closely related, such a one-base mechanism is expected to be conserved within this family of enzymes.

LITHIUM TRIENOLATE OF SORBIC ACID AS A D6 SYNTHON. SYNTHESIS OF 7-HYDROXY 2,4-DIENOIC ACIDS.

The trienolate 2 of sorbic acid is an easily available d6 synthon.Preparation of 7-hydroxy dienoic acids 5 from ketones is here described.