MUTANTS OF L-ARABINITOL 4-DEHYDROGENASE FROM NEUROSPORA CRASSA

摘要

To elucidate the determinants of substrate and cofactor recognition on LAD, the first high-resolution X-ray crystallographic structure of an LAD was determined to a resolution of 2.6. The crystal structure of the ncLAD-NAD+ complex was successfully utilized for the engineering of variants with altered cofactor specificity towards NADP+. These results provide the framework for engineering of variants with increased activity that can overcome the bottleneck in pentose catabolism in yeast.