Publications by authors named "M Kiriukhin"

Article Synopsis
  • L-serine biosynthesis starts with D-3-phosphoglycerate being converted into 3-phosphohydroxypyruvate by the enzyme SerA, which can also produce D-2-hydroxyglutarate (D-2-HGA) from 2-ketoglutarate.
  • Recent discoveries have identified bacterial enzymes called D2HGDHs that convert D-2-HGA back to 2-ketoglutarate; however, little is known about these enzymes in certain bacterial families.
  • Two novel D2HGDHs were characterized, revealing their substrate specificity, optimal pH conditions, and sensitivity to metal ions, suggesting their potential use in metabolic engineering for creating microbes with specific traits.
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The isocitrate dehydrogenase (MfIDH) with unique double coenzyme specificity from Methylobacillus flagellatus was purified and characterized, and its gene was cloned and overexpressed in E. coli as a fused protein. This enzyme is homodimeric,-with a subunit molecular mass of 45 kDa and a specific activity of 182 U mg -1 with NAD+ and 63 U mg -1 with NADP+.

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The cell energy fraction that powered maintenance and expression of genes encoding pro-phage elements, pta-ack cluster, early sporulation, sugar ABC transporter periplasmic proteins, 6-phosphofructokinase, pyruvate kinase, and fructose-1,6-disphosphatase in acetogen Clostridium sp. MT871 was re-directed to power synthetic operon encoding isobutanol biosynthesis at the expense of these genes achieved via their elimination. Genome tailoring decreased cell duplication time by 7.

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Time- and cost-efficient six-step UVC-mutagenesis was developed and validated to generate acetogen mutants with preliminary reduced genomes to prevent product inhibition in the to-be-engineered commercial biocatalysts. Genome reduction was performed via elimination of pta, ack, spo0A, spo0J and some pro-phage genes. UVC-mutants such as Clostridium sp.

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Naturally mevalonate-resistant acetogen Clostridium sp. MT1243 produced only 425 mM acetate during syngas fermentation. Using Clostridium sp.

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