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大鼠肾线粒体琥珀酰辅酶A转移酶的底物特异性

Substrate specificity of succinyl-CoA transferase from rat kidney mitochondria.

作者信息

Pacanis A, Rogulski J

出版信息

Acta Biochim Pol. 1977;24(1):3-11.

PMID:868435
Abstract
  1. Succinyl-CoA: 3-oxoacid transferase (EC 2.8.3.5) from rat kidney mitochondria, purified about 200-fold, catalyses the CoA transfer from acetoacetyl-CoA to succinate, acetoacetate, maleate, glutarate and malonate; maleate proved to be a true substrate of the enzyme. 2. Double-reciprocal plots of the initial reaction rates against substrates concentrations arb best fitted by parallel lines. Inhibition by each acid product of the reaction is competitive with respect to the acid acceptor of CoA. 3. CoA-transferase from rat kidney shows similar kinetics as, but different substrate specificity than, the enzyme from other sources.
摘要
  1. 琥珀酰辅酶A:3-氧代酸转移酶(EC 2.8.3.5),从大鼠肾脏线粒体中纯化得到,纯化倍数约为200倍,催化辅酶A从乙酰乙酰辅酶A转移至琥珀酸、乙酰乙酸、马来酸、戊二酸和丙二酸;马来酸被证明是该酶的真正底物。2. 初始反应速率对底物浓度的双倒数作图最好由平行线拟合。反应的每种酸性产物的抑制作用相对于辅酶A的酸性受体是竞争性的。3. 大鼠肾脏的辅酶A转移酶与其他来源的酶具有相似的动力学,但底物特异性不同。

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