Review of Mutarotase in 'Metabolic Subculture' and Analytical Biochemistry: Prelude to 19F NMR Studies of its Substrate Specificity and Mechanism.

This is the first paper in a sequential pair devoted to the enzyme mutarotase (aldose 1-epimerase; EC 5.1.3.3). Here, the broader context of the physiological role of mutarotase, among those enzymes considered to be part of 'metabolic structure', is reviewed. We also summarise the current knowledge about the molecular mechanism and substrate specificity of the enzyme, which is considered in the context of the binding of fluorinated glucose analogues to the enzyme's active site. This was done as a prelude to our experimental studies of the anomerisation of fluorinated sugars by mutarotase that are described in the following paper. Mutarotase (aldose 1-epimerase; EC 5.1.3.3) catalyses the rapid exchange between the α- and β-anomers of d-glucose and some other monosaccharides. We summarise current knowledge of its involvement in metabolism, and its molecular mechanism. Its substrate specificity is considered in relation to fluorinated glucose analogues reported on in the following paper. [ABSTRACT FROM AUTHOR]