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

  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},
  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.
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
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.
Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase.
Differences in coenzyme M biosynthesis afford the opportunity to develop methanogen inhibitors that discriminate between the classes of methanogenic archaea, as indicated by amino acid sequence comparison.
Purification, Overproduction, and Partial Characterization of β-RFAP Synthase, a Key Enzyme in the Methanopterin Biosynthesis Pathway†
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
ABSTRACT The products of two adjacent genes in the chromosome ofMethanococcus jannaschii are similar to the amino and carboxyl halves of phosphonopyruvate decarboxylase, the enzyme that catalyzes the
Occurrence and biosynthesis of 3-mercaptopropionic acid in Methanocaldococcus jannaschii.
It is shown that HMBA can be biosynthesized from malate semialdehyde and hydrogen sulfide, likely using a mechanism similar to that proposed for coenzyme M, coen enzyme B and homocysteine biosynthesis in methanogens, where an aldehyde is converted to a thiol.
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*
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
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.
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.


Two malate dehydrogenases in Methanobacterium thermoautotrophicum
Two malate dehydrogenases found in Methanobacterium thermoautotrophicum contain a specific for NAD+ and catalyzed the dehydrogenation of malate at approximately one-third of the rate of oxalacetate reduction, and the other could equally well use NAD + and NADP+ as coenzyme and catalyze essentially only the reduction of oxAlacetate.
Alpha-keto acid chain elongation reactions involved in the biosynthesis of coenzyme B (7-mercaptoheptanoyl threonine phosphate) in methanogenic Archaea.
The protein product of the Methanococcus jannaschii MJ0503 gene aksA (AksA) was found to catalyze the condensation of alpha-ketoglutarate and acetylCoA to form trans-homoaconitate, a precursor to coenzyme B and biotin.
Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus.
L-Malate dehydrogenase from the extremely thermophilic mathanogen Methanothermus fervidus was isolated and its phenotypic properties were characterized. The primary structure of the protein was
An evaluation of the substrate specificity and asymmetric synthesis potential of the cloned L-lactate dehydrogenase from Bacillusstearothermophilus
The potential utility of the L-lactate dehydrogenase of Bacillusstearothermophilus (BSLDH) for stereospecific, preparative-scale reductions of α-keto acids to (S)-α-hydroxy acids of > 99% ee has been
Properties and primary structure of a thermostable l-malate dehydrogenase from Archaeoglobus fulgidus
A thermostable l-malate dehydrogenase from the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus was isolated and characterized, and its gene was cloned and sequenced and shows a high similarity to l-lactate dehydrogensase from Thermotoga maritima and gram-positive bacteria.
Biosynthesis of methanopterin.
The occurrence of this pathway was confirmed by (a) the chemical and/or biochemical synthesis of most of the proposed intermediates, (b) the detection of these intermediates in cell-free extracts, and (c) the measurement of their conversion to demethylated methanopterin and/ or other intermediate in the pathway.
Elucidation of the structure of methanopterin, a coenzyme from Methanobacterium thermoautotrophicum, using two-dimensional nuclear-magnetic-resonance techniques.
Methanopterin is a coenzyme involved in methanogenesis. From 2 kg wet cells of Methanobacterium thermoautotrophicum about 35 mumol methanopterin were isolated. The structure of this compound was
Designs for a broad substrate specificity keto acid dehydrogenase.
Five changes together produced a broader substrate specificity alpha-hydroxy acid dehydrogenase, with a 55-fold improved kcat for alpha-ketoisocaproate to a value about 1/14 that of the native enzyme for pyruvate.
Proposed structure for coenzyme F420 from Methanobacterium.
The low-potential electron carrier, coenzyme F420, was purified from Methanobacterium strain M.o.H. A yield of 160 mg/kg of wet-packed cells was obtained. Results of analysis of hydrolytic fragments
NADP-malate dehydrogenase from leaves of Zea mays: purification and physical, chemical, and kinetic properties.