A study of the enzymatic inactivation of chloramphenicol by highly purified chloramphenicol acetyltransferase

Thibault, Gaétan; Guitard, Michel; Daigneault, Réjean

doi:10.1016/0005-2744(80)90223-5

Cited by 18 publications

(9 citation statements)

References 22 publications

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“…4 (25). Similarly, the transfer of acetyl groups to chloramphenicol by chloramphenicol acetyltransferase takes place by a sequential mechanism (26,27).…”

Section: Discussionmentioning

confidence: 99%

Palmitoylation of bovine opsin and its cysteine mutants in COS cells.

Karnik

Ridge

Bhattacharya

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

146

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“…4 (25). Similarly, the transfer of acetyl groups to chloramphenicol by chloramphenicol acetyltransferase takes place by a sequential mechanism (26,27).…”

Section: Discussionmentioning

confidence: 99%

Palmitoylation of bovine opsin and its cysteine mutants in COS cells.

Karnik

Ridge

Bhattacharya

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

146

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“…Two monoacetylated- 19 products were observed (Figure 3b, trace iii ), consistent with the slow noncatalytic transfer of the acetyl group from 3-acetyl- 19 to the 1-hydroxyl of 19 . 15 This then facilitated a second acetylation event at the 3-hydroxyl position, leading to production of diacetylated- 19 (Figure S14). …”

mentioning

confidence: 99%

Chemoenzymatic Synthesis of Acyl Coenzyme A Substrates Enables in Situ Labeling of Small Molecules and Proteins

Agarwal¹,

Diethelm²,

Ray³

et al. 2015

Org. Lett.

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A chemoenzymatic approach to generate fully functional acyl coenzyme A molecules that are then used as substrates to drive in situ acyl transfer reactions is described. Mass spectrometry-based assays to verify the identity of acyl coenzyme A enzymatic products are also illustrated. The approach is responsive to a diverse array of carboxylic acids that can be elaborated to their corresponding coenzyme A thioesters, with potential applications in wide-ranging chemical biology studies that utilize acyl coenzyme A substrates.

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“…However, CAT can add an acetyl only to the first acetylation site of chloramphenicol, and the second acetylation is based on re-acetylation of the first site during the non-enzymatic interconversion of mono-acetylated derivatives at higher pH values. 18) In this respect, TRI3 is a novel type of multifunctional acetylase distinct from CAT and its related acetylases, although it belongs to the CAT class of acetyltransferases containing the consensus sequence HXXXDG. 19) We also used all possible mono-and di-acetylated NIV derivatives as substrate in subsequent analyses: 3-acetylnivalenol (3-ANIV), 4-acetylnivalenol (4-ANIV), 15-ANIV, 3,4-diacetylnivalenol (3,4-diANIV), 3,15-diANIV, and 4,15-diANIV (see Fig.…”

mentioning

confidence: 99%

4-O-Acetylation and 3-O-Acetylation of Trichothecenes by Trichothecene 15-O-Acetyltransferase Encoded byFusarium Tri3

Tokai¹,

Takahashi-Ando²,

Izawa

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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In the biosynthesis of Fusarium trichothecenes, the C-3 hydroxyl group of isotrichodermol must be acetylated by TRI101 for subsequent pathway genes to function. Despite the importance of this 3-O-acetylation step in biosynthesis, Tri101 is both physically and evolutionarily unrelated to other Tri genes in the trichothecene gene cluster. To gain insight into the evolutionary history of the cluster, we purified recombinant TRI3 (rTRI3), one of the two cluster gene-encoded trichothecene O-acetyltransferases, and examined to determine whether this 15-O-acetyltransferase can add an acetyl to the C-3 hydroxyl group of isotrichodermol. When a high concentration of rTRI3 was used in the assay (final concentration, 50 M), we observed 3-Oacetylation activity against isotrichodermol that was more than 10 5 times less efficient than the known 15-Oacetylation activity against 15-deacetylcalonectrin. The rTRI3 protein also exhibited 4-O-acetylation activity when nivalenol was used as a substrate; in addition to 15-acetylnivalenol, di-acetylated derivatives, 4,15-diacetylnivalenol, and, to a lesser extent, 3,15-diacetylnivalenol, were also detected at high enzyme concentrations. The significance of the trace trichothecene 3-O-acetyltransferase activity detected in rTRI3 is discussed in relation to the evolution of the trichothecene gene cluster.

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A study of the enzymatic inactivation of chloramphenicol by highly purified chloramphenicol acetyltransferase

Cited by 18 publications

References 22 publications

Palmitoylation of bovine opsin and its cysteine mutants in COS cells.

Palmitoylation of bovine opsin and its cysteine mutants in COS cells.

Chemoenzymatic Synthesis of Acyl Coenzyme A Substrates Enables in Situ Labeling of Small Molecules and Proteins

4-O-Acetylation and 3-O-Acetylation of Trichothecenes by Trichothecene 15-O-Acetyltransferase Encoded byFusarium Tri3

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