23631-84-7Relevant articles and documents
Biocatalytic and chemical preparation of all four diastereomers of methionine sulfoxide
Holland, Herbert L.,Brown, Frances M.
, p. 535 - 538 (1998)
Biocatalytic or chemical oxidations can be used in a complementary manner for the preparation of all four diastereomers of methionine sulfoxide with high diastereomeric purity in overall isolated yields of 20-55% from methionine. The N-phthaloyl derivatives of L- and D-methionine were selectively oxidised to the (S(s)S(c)) and (S(s)R(c)) sulfoxides respectively by biotransformation using the fungus Beauveria bassiana ATCC 7159. Hydrogen peroxide oxidation of the same materials gave mixtures from which the (S(s)S(c)) and (R(s)R(c)) isomers can be readily isolated by crystallisation. Chromatography of the residual material then afforded the (R(s)S(c)) and (S(s)R(c)) isomers.
Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential
Amatuni, Alexander,Renata, Hans
, p. 1736 - 1739 (2019)
We present the functional characterization of GlbB, a lysine 4-hydroxylase from the glidobactin biosynthetic gene cluster. Despite its narrow substrate specificity, GlbB is able to catalyze the hydroxylation of l-lysine with excellent total turnover number and complete regio- and diastereoselectivity. The synthetic utility of GlbB is illustrated by its use in the efficient preparation of a key dipeptide fragment of glidobactin.
Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons
Gennaris, Alexandra,Ezraty, Benjamin,Henry, Camille,Agrebi, Rym,Vergnes, Alexandra,Oheix, Emmanuel,Bos, Julia,Leverrier, Pauline,Espinosa, Leon,Szewczyk, Joanna,Vertommen, Didier,Iranzo, Olga,Collet, Jean-Fran?ois,Barras, Frédéric
, p. 409 - 412 (2015/12/26)
The reactive species of oxygen and chlorine damage cellular components, potentially leading to cell death. In proteins, the sulfur-containing amino acid methionine is converted to methionine sulfoxide, which can cause a loss of biological activity. To res