3226-66-2

Upstream product

• 63-68-3 L-(+)-Methionine 
• 70224-21-4 (1R,3S)-dehydromethionine 
• 63-68-3 L-methionine 
• 29588-91-8 (2S)-4-methylthio-2-(1,3-dioxo-2-benzazole-2-yl)butanoic acid 
• 16639-89-7 N-Methoxycarbonyl-L-methionine 
• 158009-69-9 (2S)-methyl [2-N-(methoxycarbonyl)amino-4-(methylthio)]butanoate 
• 147059-17-4 (S_C)-N-phthaloylmethionine sulfoxide 
• 59-51-8 DL-methionine 

Relevant academic research and scientific papers

Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential

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.

Remote C-H Hydroxylation by an α-Ketoglutarate-Dependent Dioxygenase Enables Efficient Chemoenzymatic Synthesis of Manzacidin C and Proline Analogs

Selective C-H functionalization at distal positions remains a highly challenging problem in organic synthesis. Though Nature has evolved a myriad of enzymes capable of such feat, their synthetic utility has largely been overlooked. Here, we functionally characterize an α-ketoglutarate-dependent dioxygenase (Fe/αKG) that selectively hydroxylates the ? position of various aliphatic amino acids. Kinetic analysis and substrate profiling of the enzyme show superior catalytic efficiency and substrate promiscuity relative to other Fe/αKGs that catalyze similar reactions. We demonstrate the practical utility of this transformation in the concise syntheses of a rare alkaloid, manzacidin C, and densely substituted amino acid derivatives with remarkable step efficiency. This work provides a blueprint for future applications of Fe/αKG hydroxylation in complex molecule synthesis and the development of powerful synthetic paradigms centered on enzymatic C-H functionalization logic.

Synthesis of Methionine-Derived Endocyclic Sulfilimines and Sulfoximines

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.

Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons

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

Oxidation by chlorine dioxide of methionine and cysteine derivatives to sulfoxides

Methionine and cysteine derivatives were oxidized asymmetrically by chlorine dioxide to sulfinyl derivatives.

Probing the stereochemistry of the active site of gamma-glutamyl transpeptidase using sulfur derivatives of l-glutamic acid.

Gamma-glutamyl transpeptidase (GGT) catalyses the transfer of a gamma-glutamyl moiety from a donor substrate to different acceptors, such as amino acids and water. GGT is known to display relatively low stereospecificity with respect to the alpha-stereocentre of its donor substrates. In this study we have studied its stereospecificity with respect to the stereocentre at the delta-position of different analogues of L-glutamic acid. Notably, L-methionine sulfoxide is well-recognised whereas L-methionine sulfone and L-methionine sulfoximine are not. Furthermore, when the synthetic gamma-diastereoisomers of L-methionine sulfoxide were separated and tested, it was discovered that GGT shows remarkable stereospecificity at the gamma-position, binding the S(C)S(S) diastereoisomer with a K(i) of 3.5 mM, whereas the S(C)R(S) diastereoisomer is not recognised. Finally, using a sulfoxide as a new pharmacophore for GGT, we have synthesized and tested an analogue of glutathione to obtain a very promising competitive inhibitor with a K(i) of (53 +/- 3) microM.

Chloroperoxidase-catalyzed oxidation of methionine derivatives

Treatment of N-methoxycarbonyl C-carboxylate ester derivatives of L- and D-methionine and L-ethionine by chloroperoxidase-hydrogen peroxide resulted in oxidation at sulfur to produce the (RS) sulfoxide in moderate to high diastereomeric excess.

Biocatalytic and chemical routes to all the stereoisomers of methionine and ethionine sulfoxides

Biotransformations of the N-phthaloyl derivatives of D- and L-methionine and of D- and L-ethionine by Beauveria bassiana ATCC 7159 or Beauveria caledonica ATCC 64970 produce the corresponding (S(s)) sulfoxides in good yield and diastereomeric excess. Pure

Biocatalytic and chemical preparation of all four diastereomers of methionine sulfoxide

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.

A General Procedure for the Selective Oxidation of Sulfides to Sulfoxides by Nitric Acid: Tetrabromoaurate(III) Catalyst in a Biphasic System

Tetrabromoaurate(III) is an efficient catalyst for the oxidation of sulfides to sulfoxides by nitric acid in a biphasic system (nitromethane/water).The system is selective and can be applied to the oxidation of any type of dialkyl and alkyl aryl sulfide and also of diaryl sulfides activated by electron-releasing substituents.The nature of the active species has been investigated in relation to the mechanistic aspects.