117380-98-0

Basic information

• Product Name: 4-chlorobenzoyl coenzyme A
• Synonyms: 4-chlorobenzoyl coenzyme A;4-chlorobenzoyl-CoA
• CAS NO: 117380-98-0
• Molecular Formula: C₂₈H₃₉ClN₇O₁₇P₃S
• Molecular Weight: 906.085243
• Mol File: 117380-98-0.mol

Chemical Properties

• Boiling Point: °Cat760mmHg
• Flash Point: °C
• Appearance: /
• Density: 1.86g/cm³
• Refractive Index: 1.722
• PKA: 1.16±0.50(Predicted)
• CAS DataBase Reference: 4-chlorobenzoyl coenzyme A(CAS DataBase Reference)
• NIST Chemistry Reference: 4-chlorobenzoyl coenzyme A(117380-98-0)
• EPA Substance Registry System: 4-chlorobenzoyl coenzyme A(117380-98-0)

Safety Data

• Hazardous Substances Data: 117380-98-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
4-chlorobenzoyl coenzyme A is used as an intermediate in the synthesis of various pharmaceutical compounds, particularly those involving the modification or synthesis of benzoyl-CoA derivatives. Its unique structure allows for the development of new drugs with potential therapeutic benefits.
Used in Chemical Synthesis:
In the chemical industry, 4-chlorobenzoyl coenzyme A can be utilized as a key intermediate for the synthesis of a wide range of chemical products, including agrochemicals, dyes, and other specialty chemicals. Its reactivity and functional groups make it a valuable building block for creating novel compounds with specific properties.
Used in Research and Development:
4-chlorobenzoyl coenzyme A serves as an important research tool for studying the mechanisms of enzyme-catalyzed reactions and the role of coenzyme A in various biochemical pathways. It can be used to investigate the structure-activity relationships of benzoyl-CoA derivatives and their interactions with enzymes and other biomolecules.
Used in Environmental Applications:
4-chlorobenzoyl coenzyme A may also find applications in environmental science, particularly in the biodegradation of chlorinated aromatic compounds. Its ability to act as a substrate for certain enzymes could potentially be harnessed to develop bioremediation strategies for the cleanup of contaminated sites.

InChI:InChI=1/C28H39ClN7O17P3S/c1-28(2,22(39)25(40)32-8-7-18(37)31-9-10-57-27(41)15-3-5-16(29)6-4-15)12-50-56(47,48)53-55(45,46)49-11-17-21(52-54(42,43)44)20(38)26(51-17)36-14-35-19-23(30)33-13-34-24(19)36/h3-6,13-14,17,20-22,26,38-39H,7-12H2,1-2H3,(H,31,37)(H,32,40)(H,45,46)(H,47,48)(H2,30,33,34)(H2,42,43,44)/t17-,20-,21-,22+,26-/m1/s1

Upstream product

• 85-61-0 coenzyme A 
• 74-11-3 para-chlorobenzoic acid 
• 14189-18-5 4-Chlor-benzoesaeure-kohlensaeure-ethylester-anhydrid 

Downstream Products

• 4641-33-2 4-chlorobenzoate ion 
• 85-61-0 coenzyme A 
• 1215640-78-0 7,13-O,O-diacetyl-2-O-debenzoyl-2-O-(4-chlorobenzoyl)baccatin III 
• 6756-74-7 S-benzoyl coenzyme A 
• 148471-94-7 cyclohexa-1,5-diene-1-carboxyl-CoA 

Relevant articles and documents

Dehalogenation of 4-chlorobenzoate characterisation of 4-chlorobenzoyl-coenzyme a dehalogenase from pseudomonas sp. CBS3

Pseudomonas sp. CBS3 is capable of growing with 4-chlorobenzoate as sole source of carbon and energy. The removal of the chlorine of 4-chlorobenzoate is performed in the first degradation step by an enzyme system consisting of three proteins. A 4-halobenz

METHOD FOR SYNTHESISING AMIDES

The present invention relates to a method for synthesising amides that is of general applicability. The method may be performed in vitro or in vivo. Cell lines for use in the in vivo methods also form aspects of the invention. The method for synthesising a non-natural amide comprises: a. reaction of a carboxylic acid with a naturally occurring CoA ligase or a variant thereof; and b. reaction of the product of step a with an amine in the presence of a naturally occurring acyltransferase or a variant thereof; with the proviso that where the CoA ligase and acyltransferase are both naturally occurring, they are not derived from the same source species and do not act sequentially in a metabolic pathway; and with the proviso that the non-natural product is not N-(E)-p-coumaroyl-3-hydroxyanthranilic acid or N-(E)-p-caffeoyl-3-hydroxyanthranilic acid. Further, a method for producing an active pharmaceutical ingredient by the aforementioned method and host cells for carrying out said methods are envisaged.

A versatile biosynthetic approach to amide bond formation

The development of versatile and sustainable catalytic strategies for amide bond formation is a major objective for the pharmaceutical sector and the wider chemical industry. Herein, we report a biocatalytic approach to amide synthesis which exploits the diversity of Nature's amide bond forming enzymes, N-acyltransferases (NATs) and CoA ligases (CLs). By selecting combinations of NATs and CLs with desired substrate profiles, non-natural biocatalytic pathways can be built in a predictable fashion to allow access to structurally diverse secondary and tertiary amides in high yield using stoichiometric ratios of carboxylic acid and amine coupling partners. Transformations can be performed in vitro using isolated enzymes, or in vivo where reactions rely solely on cofactors generated by the cell. The utility of these whole cell systems is showcased through the preparative scale synthesis of a key intermediate of Losmapimod (GW856553X), a selective p38-mitogen activated protein kinase inhibitor.

Establishing a toolkit for precursor-directed polyketide biosynthesis: Exploring substrate promiscuities of acid-CoA ligases

Polyketides are chemically diverse and medicinally important biochemicals that are biosynthesized from acyl-CoA precursors by polyketide synthases. One of the limitations to combinatorial biosynthesis of polyketides has been the lack of a toolkit that describes the means of delivering novel acyl-CoA precursors necessary for polyketide biosynthesis. Using five acid-CoA ligases obtained from various plants and microorganisms, we biosynthesized an initial library of 79 acyl-CoA thioesters by screening each of the acid-CoA ligases against a library of 123 carboxylic acids. The library of acyl-CoA thioesters includes derivatives of cinnamyl-CoA, 3-phenylpropanoyl-CoA, benzoyl-CoA, phenylacetyl-CoA, malonyl-CoA, saturated and unsaturated aliphatic CoA thioesters, and bicyclic aromatic CoA thioesters. In our search for the biosynthetic routes of novel acyl-CoA precursors, we discovered two previously unreported malonyl-CoA derivatives (3-thiophenemalonyl-CoA and phenylmalonyl-CoA) that cannot be produced by canonical malonyl-CoA synthetases. This report highlights the utility and importance of determining substrate promiscuities beyond conventional substrate pools and describes novel enzymatic routes for the establishment of precursor-directed combinatorial polyketide biosynthesis. (Chemical Presented).

Point mutations (Q19P and N23K) increase the operational solubility of a 2α-o-benzoyltransferase that conveys various acyl groups from CoA to a taxane acceptor

Two site-directed mutations within the wild-type 2-o-benzoyltransferase (tbf) cDNA, from Taxus cuspidata plants, yielded an encoded protein containing replacement amino acids at Q19P and N23K that map to a solvent-exposed loop region. The likely significant changes in the biophysical, properties invoked by these mutations caused the overexpressed, modified TBT (mTBT) to partition into the soluble enzyme fraction about 5-fold greater than the wild-type enzyme. Sufficient protein could now be acquired to examine the scope of the substrate specificity of mTBT by incubation with 7,13-O,O-diacetyl-2-Odebenzoylbaccatin III that was mixed individually with various substituted benzoyls, alkanoyls, and (E)-butenoyl CoA donors. The mTBT catalyzed the conversion of each 7,13-O,O-diacetyl-2-O-debenzoylbaccatin III to several 7,13-O,O-diacetyl-2O- acyl-2-O-debenzoylbaeeatin III analogues. The relative catalytic efficiency of mTBT with the 7,13-O,O-diacetyl-2-Odebenzoyl surrogate substrate and heterole carbonyl CoA substrates was slightly greater than with the natural aroyl substrate benzoyl CoA, while substituted benzoyl CoA thioesters were less productive. Short-chain hydrocarbon carbonyl and cyclohexanoyl CoA thioesters were also productive, where C4 substrates were transferred by mTBT with ～10- to 17-fold greater catalytic efficiency compared to the transfer of benzoyl. The described broad specificity of mTBT suggests that a plethora of 2-O-acyl variants of the antimitotic paclitaxel can be assembled through biocatalytic sequences.