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β-Alanine Biosynthesis in Methanocaldococcus jannaschii
It was shown that the decarboxylation of aspartate was the only source of β-alanine in cell extracts of M. jannaschii, and the MJ0050 gene was demonstrated to complement the Escherichia coli panD deletion mutant cells, thus confirming the function of this gene in vivo.
Identification and characterization of a tyramine-glutamate ligase (MfnD) involved in methanofuran biosynthesis.
The identification of an ATP-grasp enzyme encoded by the gene Mefer_1180 in Methanocaldococcus fervens that catalyzes the ATP-dependent addition of one glutamate to tyramine via a γ-linked amide bond is reported, providing the first report describing the enzymology of the incorporation of the initial l-glutamate molecule into the methanofuran structure.
Mechanism of the Enzymatic Synthesis of 4-(Hydroxymethyl)-2- furancarboxaldehyde-phosphate (4-HFC-P) from Glyceraldehyde-3-phosphate Catalyzed by 4-HFC-P Synthase.
The biochemical characterization of the recombinantly expressed MfnB is described to understand its catalytic mechanism and structural analysis and molecular docking are predicted to predict the potential binding sites for two GA-3P molecules in the active site.
Biosynthesis of the 5-(Aminomethyl)-3-furanmethanol moiety of methanofuran.
We have established the biosynthetic pathway and the associated genes for the biosynthesis of the 5-(aminomethyl)-3-furanmethanol (F1) moiety of methanofuran in the methanogenic archaeon
Identification of the Final Two Genes Functioning in Methanofuran Biosynthesis in Methanocaldococcus jannaschii
The results show that MfnF catalyzes the formation of an ether bond during methanofuran biosynthesis, and further expands the functionality of this enzyme family, while MfnE is a promiscuous enzyme and its possible physiological role is to produce F1-PP.
Biochemical Characterization of a Dihydroneopterin Aldolase Used for Methanopterin Biosynthesis in Methanogens
It is proposed that in the absence of lysine, which is considered to be the general base in bacterial DHNAs, an invariant water molecule likely functions as the catalytic base, and the strictly conserved His35 and Gln61 residues serve as the hydrogen bond partners to adjust the basicity of the water molecule.
Purification, crystallization and preliminary X-ray crystallographic analysis of xylose reductase from Candida tropicalis.
The detailed three-dimensional structure ofXR will provide a better understanding of the biological significance of XR in the efficient production of xylitol from biomass.