Solution X‐ray scattering study of pig heart cytosolic aspartate aminotransferase

FEBS Letters

Arrio-Dupont, Martine²  Tardieu, Annette¹  Vergé, Daniel² 

[1] Centre de Génétique Moléculaire, CNRS, 91190 Gif sur Yvette and LURE, Bat. 209c Université Paris-Sud, 91405 Orsay, France;Laboratoire d'Enzymologie Physico-Chimique et Moléculaire, Bat. 433, Université Paris-Sud, 91405 Orsay, France

关键词: Aspartate aminotransferase;    Coenzyme binding;    Solution X-ray scattering;    Synchrotron radiation;    AAT;    aspartate aminotransferase;    SXRS;    solution X-ray scattering;    PLP;    pyridoxal 5′-phosphate;   

DOI  :  10.1016/0014-5793(83)80165-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Solution X-ray scattering experiments have been performed with apo- and holo-aspartate aminotransferase to detect the conformational change, demonstrated by a variety of techniques, induced by the binding of the coenzyme pyridoxal 5′ -phosphate to apoenzyme. The conformational change could not, in fact, be observed by solution X-ray scattering. This suggests that there is no major modification of the overall shape of the enzyme upon coenzyme binding, although there are likely to be variations in the protein—solvent interactions. An accurate value of the radius of gyration, 29.0 ± 0.5 Å has been determined.

【 授权许可】

Unknown