Abstract
The molecular structure of Taka-amylase A [EC 3.2 .1.1, Aspergillus oryzae] has been determined by X-ray crystallographic method at 3.0Å resolution . The features of the three dimensional structure and the structure similarities to other enzymes are described . The differ ence Fourier maps for the complex crystals of Taka-amylase A with substrates and inhibitors revealed their binding sites. Some experiments to confirm the homogeneity of the sample of Taka-amylase A were carried out. In order to clalify the catalytic mechanism of the enzymes on atomic level, the improvement of the X-ray structure analysis and the difference Fourier study of various complex crystals are in progress.
