95456-56-7

Basic information

• Product Name: 4-hydroxyphenylpropionyl-CoA
• Synonyms: 4-hydroxyphenylpropionyl-CoA
• CAS NO: 95456-56-7
• Molecular Weight: 915.703
• Mol File: 95456-56-7.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: 4-hydroxyphenylpropionyl-CoA(CAS DataBase Reference)
• NIST Chemistry Reference: 4-hydroxyphenylpropionyl-CoA(95456-56-7)
• EPA Substance Registry System: 4-hydroxyphenylpropionyl-CoA(95456-56-7)

Safety Data

• Hazardous Substances Data: 95456-56-7(Hazardous Substances Data)

Upstream product

• 501-97-3 4-hydroxyphenylpropionic acid 
• 85-61-0 coenzyme A 
• 30802-00-7 p-coumaroyl-coenzyme A 

Downstream Products

• 920318-17-8 dihydrobisnoryangonin 
• 60-82-2 3-(4-Hydroxy-phenyl)-1-(2,4,6-trihydroxy-phenyl)-propan-1-on 
• 5471-51-2 4-(4-hydroxyphenyl)-2-oxobutane 

Relevant articles and documents

Coenzyme A-Conjugated Cinnamic Acids – Enzymatic Synthesis of a CoA-Ester Library and Application in Biocatalytic Cascades to Vanillin Derivatives

We present a bioorthogonal method for the ligation of coenzyme A (CoA) with cinnamic acids. The reaction, which is the initial step in the biosynthesis of a multitude of bioactive secondary metabolites, is catalyzed by a promiscuous plant ligase and yields CoA conjugates with different functionalization in high purity and without formation of by-products. Its applicability in biosynthetic cascades is shown for the direct transformation of cinnamic acids into natural benzaldehydes (like vanillin) or artificial derivatives (e. g. ethylvanillin). (Figure presented.).

Rational Control of Polyketide Extender Units by Structure-Based Engineering of a Crotonyl-CoA Carboxylase/Reductase in Antimycin Biosynthesis

Bioengineering of natural product biosynthesis is a powerful approach to expand the structural diversity of bioactive molecules. However, in polyketide biosynthesis, the modification of polyketide extender units, which form the carbon skeletons, has remained challenging. Herein, we report the rational control of polyketide extender units by the structure-based engineering of a crotonyl-CoA carboxylase/reductase (CCR), in the biosynthesis of antimycin. Site-directed mutagenesis of the CCR enzyme AntE, guided by the crystal structure solved at 1.5 ? resolution, expanded its substrate scope to afford indolylmethylmalonyl-CoA by the V350G mutation. The mutant A182L selectively catalyzed carboxylation over the regular reduction. Furthermore, the combinatorial biosynthesis of heterocycle- and substituted arene-bearing antimycins was achieved by an engineered Streptomyces strain bearing AntEV350G. These findings deepen our understanding of the molecular mechanisms of the CCRs, which will serve as versatile biocatalysts for the manipulation of building blocks, and set the stage for the rational design of polyketide biosynthesis.