Molecular structure of taka-amylase A. I. Backbone chain folding at 3 A resolution

Journal of Biochemistry
Y MatsuuraM Kakudo

Abstract

The crystal structure of Taka-amylase A was studied by an X-ray diffraction method at 3 A resolution. A total of 452 amino acid residues were found from the electron density map at the present stage. The four disulfide bonds and the branched carbohydrate were also located on the map. The difference electron density map of the maltotriose-soaked crystal showed that a maltose unit was bound in the active center left. The binding of iodine atoms to the enzyme was also studied.

Citations

Mar 26, 1990·FEBS Letters·S J GamblinH C Watson
Jan 1, 1989·Critical Reviews in Biochemistry and Molecular Biology·M Vihinen, P Mäntsälä
Jan 1, 1983·Molecular and Cellular Biochemistry·K HiromiA Tanaka
Mar 23, 2013·Acta Crystallographica. Section D, Biological Crystallography·So-Young JunNam-Chul Ha
Oct 14, 2006·Molecular Microbiology·Christopher L MarionWilliam E Goldman
Jul 19, 2014·Bioscience, Biotechnology, and Biochemistry·Akihito OchiaiToshiaki Mitsui
Jan 1, 1985·Progress in Biophysics and Molecular Biology·W G Hol

Related Concepts

Mégamylase
Amylases
Aspergillus oryzae
Disulfides
Fast Electrons
Protein Conformation
X-Ray Diffraction

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