Tobimatsu T, Kajiura H, Yunoki M, Azuma M, Toraya T
Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, Tsushima-Naka, Okayama 700-8530, Japan.
J Bacteriol. 1999 Jul;181(13):4110-3. doi: 10.1128/JB.181.13.4110-4113.1999.
Adenosylcobalamin-dependent glycerol dehydratase undergoes inactivation by glycerol, the physiological substrate, during catalysis. In permeabilized cells of Klebsiella pneumoniae, the inactivated enzyme is reactivated in the presence of ATP, Mg2+, and adenosylcobalamin. We identified the two open reading frames as the genes for a reactivating factor for glycerol dehydratase and designated them gdrA and gdrB. The reactivation of the inactivated glycerol dehydratase by the gene products was confirmed in permeabilized recombinant Escherichia coli cells coexpressing GdrA and GdrB proteins with glycerol dehydratase.
腺苷钴胺素依赖性甘油脱水酶在催化过程中会被其生理底物甘油失活。在肺炎克雷伯菌的透化细胞中,失活的酶在ATP、Mg2+和腺苷钴胺素存在的情况下会重新激活。我们将两个开放阅读框鉴定为甘油脱水酶再激活因子的基因,并将它们命名为gdrA和gdrB。在与甘油脱水酶共表达GdrA和GdrB蛋白的透化重组大肠杆菌细胞中,证实了基因产物对失活甘油脱水酶的再激活作用。