Article
L-allo-threonine aldolase with an H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity.
Acta crystallographica. Section D, Biological crystallography - 1 Jun 2014
Qin Hui-Min, Imai Fabiana Lica, Miyakawa Takuya, Kataoka Michihiko, Kitamura Nahoko, Urano Nobuyuki, Mori Koji, Kawabata Hiroshi, Okai Masahiko, Ohtsuka Jun, Hou Feng, Nagata Koji, Shimizu Sakayu, Tanokura Masaru
Abstract excerpt
L-allo-Threonine aldolase (LATA), a pyridoxal-5'-phosphate-dependent enzyme from Aeromonas jandaei DK-39, stereospecifically catalyzes the reversible interconversion of L-allo-threonine to glycine and acetaldehyde. Here, the crystal structures of LATA and its mutant LATA_H128Y/S292R were determined at 2.59 and 2.50 Å resolution, respectively. Their structures implied that conformational changes in the loop...
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