Lin T W, Bridger W A
Department of Biochemistry, University of Alberta, Edmonton, Canada.
J Biol Chem. 1992 Jan 15;267(2):975-8.
We have isolated a full-length cDNA clone encoding the cytoplasmic precursor to pig heart mitochondrial CoA transferase (succinyl-CoA:3-ketoacid coenzyme A transferase (3-oxoacid CoA transferase, EC 2.8.3.5], a key enzyme for ketone body catabolism. The deduced amino acid sequence indicates the presence of a 39-residue mitochondrial signal sequence and a 481-residue mature protein of molecular weight 52,197. CoA transferase is known to be susceptible to proteolytic cleavage to produce a nicked but active enzyme. We have identified the site of proteolysis, and analysis of the sequence in its vicinity suggests that the polypeptide may fold into two domains connected by a highly hydrophilic bridge.
我们分离出了一个全长cDNA克隆,它编码猪心脏线粒体辅酶A转移酶(琥珀酰辅酶A:3-酮酸辅酶A转移酶(3-氧代酸辅酶A转移酶,EC 2.8.3.5))的胞质前体,该酶是酮体分解代谢的关键酶。推导的氨基酸序列表明存在一个39个残基的线粒体信号序列和一个分子量为52,197的481个残基的成熟蛋白。已知辅酶A转移酶易受蛋白水解切割,产生一种有缺口但有活性的酶。我们已经确定了蛋白水解位点,对其附近序列的分析表明,该多肽可能折叠成由高度亲水桥连接的两个结构域。