The effect of EDTA on the apparent hysteretic properties of pyruvate carboxylase from Rhizopus arrhizus

FEBS Letters

Scrutton, Michael C.¹  Osmani, Stephen A.¹ 

[1] Department of Biochemistry, King's College, Strand, London WC2R 2LS, England

关键词: Pyruvate carboxylase;    Rhizopus arrhizus;    Acetyl-CoA;    L-Aspartate;    EDTA;    Regulation;   

DOI  :  10.1016/0014-5793(84)81002-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Pyruvate carboxylase purified from Rhizopus arrhizus in the presence of 1 mM EDTA shows markedly nonlinear progress curves when assayed in the presence of acetyl-CoA (activator) or L-aspartate (inhibitor). The non-linear progress curves are not abolished by preincubation of the enzyme with substrates, activator or inhibitor. Activation by acetyl-CoA is prevented and can be reversed by the addition of EDTA. Enzyme purified in the absence of EDTA is immediately responsive to activation by acetyl-CoA and inhibition by L-aspartate and shows linear progress curves. Incubation of such an enzyme with EDTA induces properties characteristic of the preparation purified in the presence of this chelating agent. Tight binding of EDTA to the enzyme could not be demonstrated.

【 授权许可】

Unknown