- An Acyl Transfer Reaction Catalyzed by an Epimerase MarH
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MarH, a small protein (129 amino acids) belonging to the cupin superfamily, was previously characterized as an epimerase involved in the (2S,3S)-β-methyltryptophan formation in the maremycin biosynthesis. Here, MarH was discovered to act as an acyltransferase that can catalyze the 3-O-acylation of chloramphenicol. Furthermore, MarH can catalyze N-acylation of deacylated chloramphenicol analogue thereby activating them for 3-O-acylation. By systematic site-directed mutagenesis, H64 was revealed as a potential catalytic base that deprotonates the acyl acceptor substrate. Nucleophilic attack at the carbonyl carbon of the acyl donor then gives the acylation product.
- Han, Mo,Yin, Haixing,Zou, Yi,Brock, Nelson L.,Huang, Tingting,Deng, Zixin,Chu, Yiwen,Lin, Shuangjun
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p. 788 - 792
(2016/02/18)
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- A short asymmetric total synthesis of chloramphenicol using a selectively protected 1,2-diol
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A general route for the synthesis of chloramphenicol, thiamphenicol and fluoramphenicol is described. Chloramphenicol has been synthesized in 45% overall yield.
- Boruwa, Joshodeep,Borah, Jagat C.,Gogoi, Siddhartha,Barua, Nabin C.
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p. 1743 - 1746
(2007/10/03)
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- Stereoselective synthesis of chloramphenicol from D-serine
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An efficient synthesis of the widely used antibiotic chloramphenicol (1) is described. The key step in the synthesis involves chelation-controlled addition of phenylmagnesium bromide to a suitably protected D-serinal derivative, affording the pivotal D-threo 1,2-amino alcohol intermediate 3 in a highly stereoselective manner.
- Veeresa,Datta, Apurba
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p. 8503 - 8004
(2007/10/03)
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