Science Tokyo Archives - Astrobiology

A Overlay of the base binding pockets of MAN (AlphaFold3 structure AF-A0A2T5C445-F1-v4)77 and CHU (PDB ID 6AN9)19. Conserved residues other than H118, R117, and N138 that mediate binding are not drawn. Sequence differences in the primary base binding pocket are drawn as cyan and magenta sticks for CHU and MAN, respectively. Sequence differences involving residues that point away from the base binding pocket and were not characterized further are shown as yellow sticks. AF3 models of MAN bound to all four nucleotides are presented in Supplementary Fig. 10. Additional sequence information can be found in Fig. 1C. B Characterization of position 138. Note that activities are normalized to MAN activity, indicated by the fuchsia outer ring. C Characterization of base binding site chimeras. Refer to the main text for more details. D Overlay of the polyphosphate binding track, following the coloring conventions in (A). E Characterization of polyphosphate binding site chimera. C and E report the percentage of NTP production. Plotted values are the average of 4 independent runs. Error bars are standard deviations. Source data for this figure is available in the Source Data file. 00 Institute of Science Tokyo

Biochemistry & Organic Chemistry, Biophysics, Biosignatures & Paleobiology, Genomics, Proteomics, Bioinformatics, Press Release

Discovery Of A Universal Enzyme That Makes All Four Nucleotide Building Blocks Of Life

by Keith CowingApril 15, 2026April 15, 2026

A bacterial enzyme called universal PPK2 may simplify and lower the cost of RNA synthesis.