Korsova T L, Karagodina Z V, Poznanskaia A A, Iakovlev V A
Biokhimiia. 1979 Mar;44(3):467-76.
The interaction of AdoCbl-dependent glycerol dehydratase with the substrates (glycerol, 1,2-propandiol, ethylene glycol) and their analogs (aliphatic diols) was studied kinetically. It was found that all the diols tested are competitive inhibitors of the enzyme with respect to substrates. The arrangement of hydroxyl groups in the molecule, the length of the carbohydrate chain and the nature of the substituent at the C-3 atom are essential for the binding of diol in the active center. The ternary enzyme-AdoCbl-substrate (analog) complexes are subjected to specific inactivation at a rate, which depends on the chemical structure of the substrate (analog). The constants for inactivation and dissociation of the ternary complexes were determined. It was shown that in contrast to the double complexes (enzyme-AdoCbl), the inactivation of the ternary complexes does not depend on oxygen. Some aspects of the mechanism of specific inactivation of glycerol dehydratase are discussed.
对依赖腺苷钴胺素的甘油脱水酶与底物（甘油、1,2 - 丙二醇、乙二醇）及其类似物（脂肪族二醇）之间的相互作用进行了动力学研究。结果发现，所有测试的二醇相对于底物而言都是该酶的竞争性抑制剂。分子中羟基的排列、碳水化合物链的长度以及C - 3原子上取代基的性质对于二醇在活性中心的结合至关重要。三元酶 - 腺苷钴胺素 - 底物（类似物）复合物会以一定速率发生特异性失活，该速率取决于底物（类似物）的化学结构。测定了三元复合物的失活常数和解离常数。结果表明，与二元复合物（酶 - 腺苷钴胺素）不同，三元复合物的失活不依赖于氧气。文中还讨论了甘油脱水酶特异性失活机制的一些方面。
