Scamuffa M D, Caprioli R M
Biochim Biophys Acta. 1980 Aug 7;614(2):583-90. doi: 10.1016/0005-2744(80)90247-8.
Escherichia coli grown on gluconeogenic compounds as carbon sources produced two chemically and physically distinct types of fructose-1,6-biphosphate aldolases (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphatelyase, EC 4.1.2.13), while these bacteria produced only a single enzyme when grown on glucose or fructose. We have investigated this enzyme in several strains of Escherichia coli (Crookes, K-12, and B) grown on glucose, fructose lactate, pyruvate, alanine and glycerol by comparing chemical properties and mechanisms of action. Comparison of these mechanisms was accomplished by following the fate of 18O in the keto position of fructose 1,6-bisphosphate during the aldolase catalyzed cleavage reaction. The results show that the two enzymes have different mechanisms of action and are consistent with a Schiff-base mechanism for the one which was induced by gluconeogenic substrates and metal-chelate mechanism for the constitutive enzyme.
以糖异生化合物作为碳源生长的大肠杆菌产生了两种化学和物理性质不同的1,6-二磷酸果糖醛缩酶（D-果糖-1,6-二磷酸-D-甘油醛-3-磷酸裂解酶，EC 4.1.2.13），而这些细菌在以葡萄糖或果糖为碳源生长时只产生一种酶。我们通过比较几种在葡萄糖、果糖、乳酸、丙酮酸、丙氨酸和甘油上生长的大肠杆菌菌株（克鲁克斯、K-12和B）中该酶的化学性质和作用机制进行了研究。这些机制的比较是通过在醛缩酶催化的裂解反应过程中追踪1,6-二磷酸果糖酮基位置上18O的去向来完成的。结果表明，这两种酶具有不同的作用机制，这与由糖异生底物诱导产生的那种酶的席夫碱机制以及组成型酶的金属螯合机制是一致的。
