3226-66-2Relevant articles and documents
Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential
Amatuni, Alexander,Renata, Hans
supporting information, p. 1736 - 1739 (2019/02/20)
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.
Synthesis of Methionine-Derived Endocyclic Sulfilimines and Sulfoximines
Marzag, Hamid,Schuler, Marie,Tatibou?t, Arnaud,Reboul, Vincent
supporting information, p. 896 - 900 (2017/02/15)
The asymmetric synthesis of endocyclic methionine sulfilimines and sulfoximines from methionine derivatives was explored. The cyclization was performed by using phenyliodine diacetate (PIDA). In the case of l-methionine, dehydromethionine was obtained, and a deprotonation step by tBuONa was necessary to yield the corresponding sulfilimine. On the other hand, the cyclic sulfilimine of methionine methyl ester, methylthiopropylamine, and l-methioninol were synthesized in a single step by using PIDA. Owing to their instability, the sulfilimines were oxidized to their corresponding sulfoximines in good yields.
Oxidation by chlorine dioxide of methionine and cysteine derivatives to sulfoxides
Loginova,Rubtsova,Kuchin
experimental part, p. 752 - 754 (2009/05/09)
Methionine and cysteine derivatives were oxidized asymmetrically by chlorine dioxide to sulfinyl derivatives.