人类丙酮酸激酶缺乏症中的丙酮酸激酶单体形式。
A monomeric form of pyruvate kinase in human pyruvate kinase deficiency.
作者信息
Adachi K, Ghory P K, Asakura T, Schwartz E
出版信息
Proc Natl Acad Sci U S A. 1977 Feb;74(2):501-4. doi: 10.1073/pnas.74.2.501.
A mutant pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) from human erythrocytes which is easily separated into monomers and dimers by gel chromatography is described. Tht mutant enzyme shows almost the same pH optimum and thermostability as normal enzyme, but has a decreased stability on shaking with air, a decreased Km for phosphoenolpyruvate and a loss of allosteric properties. The apparent Km values for phosphoenolpyruvate of tetramers and monomers were the same. The tetrameric enzyme was slightly activated by fructose-1,6-diphosphate but the monomeric form was not. The tetrameric enzyme was found to dissociate spontaneously to dimeric and monomeric forms.
本文描述了一种来自人红细胞的突变型丙酮酸激酶（ATP：丙酮酸2-O-磷酸转移酶，EC 2.7.1.40），它通过凝胶色谱法很容易分离成单体和二聚体。该突变酶的最适pH值和热稳定性与正常酶几乎相同，但在与空气振荡时稳定性降低，对磷酸烯醇丙酮酸的Km值降低，且丧失了别构性质。四聚体和单体对磷酸烯醇丙酮酸的表观Km值相同。四聚体酶被1,6-二磷酸果糖轻微激活，但单体形式则不然。发现四聚体酶会自发解离为二聚体和单体形式。
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