Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme Biosynthesis in Methanoarchaea

@article{Graupner2000IdentificationOA,
  title={Identification of an Archaeal 2-Hydroxy Acid Dehydrogenase Catalyzing Reactions Involved in Coenzyme Biosynthesis in Methanoarchaea},
  author={Marion Graupner and Huimin Xu and Robert H. White},
  journal={Journal of Bacteriology},
  year={2000},
  volume={182},
  pages={3688 - 3692}
}
ABSTRACT Two putative malate dehydrogenase genes, MJ1425 and MJ0490, fromMethanococcus jannaschii and one from Methanothermus fervidus were cloned and overexpressed in Escherichia coli, and their gene products were tested for the ability to catalyze pyridine nucleotide-dependent oxidation and reduction reactions of the following α-hydroxy–α-keto acid pairs: (S)-sulfolactic acid and sulfopyruvic acid; (S)-α-hydroxyglutaric acid and α-ketoglutaric acid; (S)-lactic acid and pyruvic acid; and 1… 
L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii.
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It is reported that 6-deoxy-5-ketofructose 1-phosphate and l-aspartate semialdehyde are precursors to DHQ, consistent with the remaining steps and genes in the pathway being the same as in the established shikimate pathway.
Expression, Purification, and Characterization of (R)-Sulfolactate Dehydrogenase (ComC) from the Rumen Methanogen Methanobrevibacter millerae SM9
TLDR
The critical role of ComC in two separate cofactor pathways makes this enzyme a potential means of developing methanogen-specific inhibitors for controlling ruminant methane emissions which are increasingly being recognized as contributing to climate change.
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TLDR
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Purification, Overproduction, and Partial Characterization of β-RFAP Synthase, a Key Enzyme in the Methanopterin Biosynthesis Pathway†
TLDR
The identification of a gene encoding a potential beta-RFAP synthase in M. extorquens is the first report of a putative methanopterin biosynthetic gene found in the Bacteria and provides evidence that the pathways of methanpterin biosynthesis in B bacteria and Archaea are similar.
Identification of the Gene Encoding Sulfopyruvate Decarboxylase, an Enzyme Involved in Biosynthesis of Coenzyme M
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Occurrence and biosynthesis of 3-mercaptopropionic acid in Methanocaldococcus jannaschii.
TLDR
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The Putative Malate/Lactate Dehydrogenase from Pseudomonas putida Is an NADPH-dependent Δ1-Piperideine-2-carboxylate/Δ1-Pyrroline-2-carboxylate Reductase Involved in the Catabolism of d-Lysine and d-Proline*
TLDR
The enzyme has dual metabolic functions, and is named Δ1-piperideine-2-carboxylate/Δ1- pyrroline- 2-car boxylate reductase, the first member of a novel subclass in a large family of NAD(P)-dependent oxidoreductases.
Identification of Lactaldehyde Dehydrogenase in Methanocaldococcus jannaschii and Its Involvement in Production of Lactate for F420 Biosynthesis
TLDR
Preliminary studies had shown that L-lactate in M. jannaschii is not derived from pyruvate, and thus an alternate pathway(s) for its formation was examined, and here it is reported that it is formed by the NAD(+)-dependent oxidation of l- lactaldehyde by the MJ1411 gene product.
Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. A member of a new class of Mg(2+)-dependent acid phosphatases.
TLDR
The broad and disparate distribution of comB homologs suggests that the gene has been recruited frequently into new metabolic pathways, and has a low pH optimum for activity, a narrow substrate specificity and an amino acid sequence dissimilar to any biochemically characterized protein.
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