アスパラギン合成酵素の結晶構造 : II型アミノアシル-tRNA合成酵素との進化上の関係 Crystal Structure of Asparagine Synthetase-Evolutional Relationship to Class II Aminoacyl-tRNA Synthetase
The crystal structure of <I>Eschelichia coli</I> asparagine synthetase has been determined by X-ray diffraction analysis. The overall structure of the enzyme is remarkably similar to that of the catalytic domain of yeast aspartyl-tRNA synthetase despite low sequence similarity (11%) . These enzymes have a commom reaction mechanism that implies the formation of an aminoacyl-adenylate intermediate. The active site architecture and most of the catalytic residues are also conserved in both enzymes. These proteins have probably evolved from a common ancester even though their sequence similarities are small.
日本結晶学会誌 41(2), 129-135, 1999-04-28
The Crystallographic Society of Japan