10318-16-8Relevant articles and documents
Fluorinated chloramphenicol acetyltransferase thermostability and activity profile: Improved thermostability by a single-isoleucine mutant
Voloshchuk, Natalya,Lee, Man Xia,Zhu, Wan Wen,Tanrikulu, Ismet Caglar,Montclare, Jin Kim
, p. 5907 - 5911 (2007)
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.
Gross, Frank,Lewis, Elizabeth A,Piraee, Mahmood,van Pee, Karl-Heinz,Vining, Leo C,White, Robert L
, p. 283 - 286 (2002)
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
Xun, Jin,Huang, Haidong,Vogel, Kurt W.,Drueckhammer, Dale G.
, p. 90 - 107 (2005)
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
Bizerra, Ayla M.C.,Montenegro, Tasso G.C.,Lemos, Telma L.G.,De Oliveira, Maria C.F.,De Mattos, Marcos C.,Lavandera, Iván,Gotor-Fernández, Vicente,De Gonzalo, Gonzalo,Gotor, Vicente
, p. 2858 - 2862 (2011/05/12)
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.