Baldwin S A, Perham R N
Biochem J. 1978 Mar 1;169(3):643-52. doi: 10.1042/bj1690643.
Investigation of aldolase 1, the class-I D-fructose 1,6-bisphosphate aldolase (EC4.1.2.13) from Escherichia coli (Crookes' strain), showed it to have unusual kinetic and structural properties. The enzyme appeared to be larger than was previously supposed and may be a decamer with a mol. wt. of approx. 340000. Its fructose 1,6-bisphosphate-cleavage activity was unaffected by these compounds. The enhancement exhibited a strong dependence on pH. These novel kinetic properties do not seem to be shared by any other fructose 1,6-bisphosphate aldolase, but recall the activation by polycarboxylic acids of the deoxyribose 3-phosphate aldolases from some other organisms. In view of its unusual properties, it is unlikely that aldolase 1 from E. coli is closely related to the class-1 aldolases that have been detected in several other prokaryotes, or to the typical class-1 enzymes from eukaryotes.
对来自大肠杆菌（克鲁克斯菌株）的I类D-果糖1,6-二磷酸醛缩酶（EC4.1.2.13）醛缩酶1的研究表明，它具有不同寻常的动力学和结构特性。该酶似乎比之前认为的要大，可能是一种分子量约为340000的十聚体。其果糖1,6-二磷酸裂解活性不受这些化合物的影响。这种增强表现出对pH的强烈依赖性。这些新的动力学特性似乎不为任何其他果糖1,6-二磷酸醛缩酶所共有，但让人想起其他一些生物体中多羧酸对脱氧核糖3-磷酸醛缩酶的激活作用。鉴于其不同寻常的特性，大肠杆菌的醛缩酶1不太可能与在其他几种原核生物中检测到的I类醛缩酶，或与真核生物中的典型I类酶密切相关。
