Human Metabolome Database: Showing metabocard for 2-Oxo-4-methylthiobutanoic acid (HMDB0001553)
2-Keto-4-(Methylthio)Butyric Acid (Keto Analog of Methionine) Is a Safe and Efficacious Precursor of l-Methionine in Chicks | Request PDF
4-(Methylsulfanyl)-2-oxobutanoic acid | C5H8O3S - PubChem
4-(Methylsulfanyl)-2-oxobutanoic acid | C5H8O3S | CID 473 - structure, chemical names, physical and chemical properties, classification, patents, literature, biological activities, safety/hazards/toxicity information, supplier lists, and more.
2-Keto-4-(Methylthio)Butyric Acid (Keto Analog of Methionine) Is a Safe and Efficacious Precursor of l-Methionine in Chicks | The Journal of Nutrition | Oxford Academic
Abstract. Relative bioefficacy and toxicity of Met precursor compounds were investigated in young chicks. The effectiveness of dl-Met and 2-keto-4-(methylthio)b
One-Step Biosynthesis of α-Keto-γ-Methylthiobutyric Acid from L-Methionine by an Escherichia coli Whole-Cell Biocatalyst Expressing an Engineered L-Amino Acid Deaminase from Proteus vulgaris
α-Keto-γ-methylthiobutyric acid (KMTB), a keto derivative of -methionine, has great potential for use as an alternative to -methionine in the poultry industry and as an anti-cancer drug. This study developed an environment friendly process ...
One-Step Biosynthesis of α-Keto-γ-Methylthiobutyric Acid from L-Methionine by an Escherichia coli Whole-Cell Biocatalyst Expressing an Engineered L-Amino Acid Deaminase from Proteus vulgaris
α-Keto-γ-methylthiobutyric acid (KMTB), a keto derivative of l-methionine, has great potential for use as an alternative to l-methionine in the poultry industry and as an anti-cancer drug. This study developed an environment friendly process for KMTB production from l-methionine by an Escherichia coli whole-cell biocatalyst expressing an engineered l-amino acid deaminase (l-AAD) from Proteus vulgaris. We first overexpressed the P. vulgaris l-AAD in E. coli BL21 (DE3) and further optimized the whole-cell transformation process. The maximal molar conversion ratio of l-methionine to KMTB was 71.2% (mol/mol) under the optimal conditions (70 g/L l-methionine, 20 g/L whole-cell biocatalyst, 5 mM CaCl2, 40°C, 50 mM Tris-HCl [pH 8.0]). Then, error-prone polymerase chain reaction was used to construct P. vulgaris l-AAD mutant libraries. Among approximately 104 mutants, two mutants bearing lysine 104 to arginine and alanine 337 to serine substitutions showed 82.2% and 80.8% molar conversion ratios, respectively. Furthermore, the combination of these mutations enhanced the catalytic activity and molar conversion ratio by 1.3-fold and up to 91.4% with a KMTB concentration of 63.6 g/L. Finally, the effect of immobilization on whole-cell transformation was examined, and the immobilized whole-cell biocatalyst with Ca2+ alginate increased reusability by 41.3% compared to that of free cell production. Compared with the traditional multi-step chemical synthesis, our one-step biocatalytic production of KMTB has an advantage in terms of environmental pollution and thus has great potential for industrial KMTB production.