Interaction of AMP with cytosolic apo‐aspartate aminotransferase

FEBS Letters

Garzillo, A.M.¹  Marino, G.¹  Di Donato, A.¹  Fiore, R.¹ 

[1] Istituto di Chimica Organica e Biologica, Università di Napoli, Via Mezzocannone 16, I-80134 Naples, Italy

关键词: AMP;    Aspartate aminotransferase;    Pyridoxal-5′-phosphate;    PLP;    pyridoxal-5′-phosphate;   

DOI  :  10.1016/0014-5793(83)80126-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Interaction of cytosolic apo-aspartate aminotransferase with AMP has been studied under equilibrium conditions: e.g., equilibrium dialysis and spectrophotometric titration. Results show that a 1:1 stoichiometric complex AMP—apo-aspartate aminotransferase monomer is formed. The calculated dissociation constants with the two different experimental techniques are 40.4 × 10⁻⁶ M⁻¹ and 31.4 × 10⁻⁶ M⁻¹, respectively. These findings substantiate a previous hypothesis of control of the reconstitution of cytosolic apo-aspartate aminotransferases exerted by AMP.

【 授权许可】

Unknown