Hayao Taguchi

TL;DR: The gene encoding D-lactate dehydrogenase of Lactobacillus plantarum has been sequenced, and expressed in Escherichia coli cells with an inducible expression plasmid, in which the 5'-noncoding region of the gene was replaced with the tac promoter, suggesting that the new family consists of D-isomer-stereospecific enzymes.

TL;DR: The enzyme contained four Cys residues (probably as two cystines), and its amino acids composition was similar to those of cysteine-containing serine proteases (proteinase K, etc.) as well as those of subtilisins, and the NH2-terminal sequence of aqualysin I showed homology with those of the microbial serines.

TL;DR: It is revealed that p94 binds to connectin at multiple sites, including newly identified loci in the N2A and PEVK regions of connectin, which supports a model in which MARP2-p94 signaling converges within the N 2A connectin segment and the mdm deletion disrupts their coordination.

TL;DR: The results indicate that the T: litoralis enzyme catalyzes not only intermolecular transglycosylation to produce linear α-1,4-glucan, but also intramolecular transmutation to produce cycloamylose, similarly to potato 4-α- glucanotransferase (called disproportionating enzyme).

TL;DR: Heat-stable L-lactate dehydrogenase was purified from an extremely thermophilic bacterium belonging to the genus Thermus, and it showed an allosteric nature dependent on fructose 1,6-bisphosphate as an effector.