10318-16-8

Basic information

• Product Name: chloramphenicol 3-acetate
• Synonyms: chloramphenicol 3-acetate;3-O-AcetylchloraMphenicol, ChloraMphenicol 3-acetate;ChloraMphenicol acetate
• CAS NO: 10318-16-8
• Molecular Formula: C₁₃H₁₄Cl₂N₂O₆
• Molecular Weight: 365.16606
• Mol File: 10318-16-8.mol
• Article Data: 8

Chemical Properties

• Boiling Point: 589°C at 760 mmHg
• Flash Point: 310°C
• Appearance: /
• Density: 1.473g/cm³
• Vapor Pressure: 1.02E-14mmHg at 25°C
• Refractive Index: 1.576
• Storage Temp.: -20°C Freezer
• Solubility: Chloroform (Slightly), Methanol (Slightly)
• CAS DataBase Reference: chloramphenicol 3-acetate(CAS DataBase Reference)
• NIST Chemistry Reference: chloramphenicol 3-acetate(10318-16-8)
• EPA Substance Registry System: chloramphenicol 3-acetate(10318-16-8)

Safety Data

• Hazardous Substances Data: 10318-16-8(Hazardous Substances Data)

Usage

Description

Chloramphenicol acetate is an acetylated and inactive version of chloramphenicol. It is formed in E. coli and S. aureus by the inducible enzyme chloramphenicol acetyltransferase in the presence of acetyl coenzyme A (acetyl-CoA; ) to confer chloramphenicol resistance. Chloramphenicol acetate has no antibiotic activity against S. sonnei in a turbidimetric assay.

Uses

Different sources of media describe the Uses of 10318-16-8 differently. You can refer to the following data:
1. Chloramphenicol acetate is a naturally-occurring co-metabolite of chloramphenicol in Streptomyces venezuelae with albeit significantly lower potency. Chloramphenicol acetate is the major product of chloramphenicol acetyltransferase, the major resistance mechanism to chloramphenicol.
2. Chloramphenicol 3-Acetate is an Chloramphenicol (C325030) derivative found in metabolic decomposition of Chloramphenicol by Alcaligenes faecalis.

InChI:InChI=1/C13H14Cl2N2O6/c1-7(18)23-6-10(16-13(20)12(14)15)11(19)8-2-4-9(5-3-8)17(21)22/h2-5,10-12,19H,6H2,1H3,(H,16,20)/t10-,11-/m1/s1

Upstream product

• 56-75-7 chloramphenicol 
• 72-89-9 acetylcoenzyme A 
• 10318-17-9 (1R,2R)-3-(acetyloxy)-2-[(dichloroacetyl)amino]-1-(4-nitrophenyl)propyl acetate 
• 108-05-4 vinyl acetate 
• 72-89-9 S-acetyl coenzyme A 
• 851986-97-5 C₂₄H₄₀N₇O₁₇P₃S 
• 851986-96-4 C₂₃H₃₇N₆O₁₈P₃S 
• 108-24-7 acetic anhydride 
• 79-20-9 acetic acid methyl ester 
• 56-75-7 2-(2,2-dichloroacetylamino)-1-(4-nitrophenyl)propane-1,3-diol 
• 75-36-5 acetyl chloride 
• 51146-98-6 3-acetoxy-2-(2,2-dichloro-acetylamino)-1-(4-nitro-phenyl)-propan-1-one 

Downstream Products

• 119-62-0 (1RS,2SR)-2-amino-1-(4-nitro-phenyl)-propane-1,3-diol 

Relevant articles and documents

Fluorinated chloramphenicol acetyltransferase thermostability and activity profile: Improved thermostability by a single-isoleucine mutant

A lysate-based thermostability and activity profile is described for chloramphenicol acetyltransferase (CAT) expressed in trifluoroleucine, T (CAT T). CAT and 13 single-isoleucine CAT mutants were expressed in medium supplemented with T and assayed for thermostability on cell lysates. Although fluorinated mutants, L82I T and L208I T, showed losses in thermostability, the L158I T fluorinated mutant demonstrated an enhanced thermostability relative to CAT T. Further characterization of L158I T suggested that T at position 158 contributed to a portion of the observed loss in thermostability upon global fluorination.

Isolation of 3' -O-acetylchloramphenicol: a possible intermediate in chloramphenicol biosynthesis.

3' -O-acetylchloramphenicol, commonly formed from chloramphenicol by resistant bacteria, has been isolated from the antibiotic-producing organism. Biosynthetic experiments suggest that it is a protected intermediate in chloramphenicol biosynthesis, implicating acetylation as a self-resistance mechanism in the producing organism.

The importance of the amide bond nearest the thiol group in enzymatic reactions of coenzyme A

Analogues of coenzyme A (CoA) and of CoA thioesters have been prepared in which the amide bond nearest the thiol group has been modified. An analogue of acetyl-CoA in which this amide bond is replaced with an ester linkage was a good substrate for the enzymes carnitine acetyltransferase, chloramphenicol acetyltransferase, and citrate synthase, with Km values 2- to 8-fold higher than those of acetyl-CoA and Vmax values from 14 to >80% those of the natural substrate. An analogue in which an extra methylene group was inserted between the amide bond and the thiol group showed less than 4-fold diminished binding to the three enzymes but exhibited less than 1% activity relative to acetyl-CoA with carnitine acetyltransferase and no measurable activity with the other two enzymes. Analogues of several CoA thioesters in which the amide bond was replaced with a hemithioacetal linkage exhibited no measurable activity with the appropriate enzymes. The results indicate that some aspects of the amide bond and proper distance between this amide and the thiol/thioester moiety are critical for activity of CoA ester-utilizing enzymes.

Enzymatic regioselective production of chloramphenicol esters

An enzymatic study has been performed in the search for synthetic routes to produce chloramphenicol derivatives through regioselective processes using lipases. Complementary transesterification and hydrolytic reactions have been carried to synthesize chloramphenicol regioisomers. Reaction parameters, such as biocatalyst, solvent, acyl donor, and temperature have been optimised in order to obtain chloramphenicol esters with high yields through acylation processes. Scale-up of the enzymatic reactions (1 g-scale at 0.25 M) and catalyst recycling (up to 10 cycles) have been successfully achieved. Furthermore, monoacylated derivatives at the more hindered secondary position could also be obtained employing hydrolysis processes.