Abstract
Hexokinase (ATP: D-hexose 6-phosphotransferase, EC2.7.1.1) and glycerol kinase (ATP: glycerol phosphotransferase, EC2.7.1.30) catalyze the phosphorylation of their respective hexose and triose substrates in order to initiate mammalian metabolism of these compounds. The priority of these enzymes in metabolism alone would make them worthy subjects of investigation. For many of us, however, their interest also lies in their “social relations in the cell” as Kornberg (1989) so nicely stated. There is abundant evidence that hexokinase and glycerol kinase interact with porin, the voltage-dependent anion-selective channel (VDAC) of the outer mitochondrial membrane, in a developmental stage and tissue specific manner in the normal individual (McCabe 1983; Adams et al 1991a). There is also evidence that binding is altered in certain disease states. We will discuss the role of the porin-kinase interactions in a variety of diseases and the metabolic impact of these interactions, or, in some cases, their disruption.
Beyond the catalytic activities of these assemblies and the factors that fine-tune their operations, we need to be aware of their social relations in the cell — their attachments to other protein units, to membranes, and to the skeletal framework., A. Kornberg in For the Love of Enzymes (1989)
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Adams, V., McCabe, E.R.B. (1994). Role of Porin-Kinase Interactions in Disease. In: Forte, M., Colombini, M. (eds) Molecular Biology of Mitochondrial Transport Systems. NATO ASI Series, vol 83. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78936-6_25
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DOI: https://doi.org/10.1007/978-3-642-78936-6_25
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