Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 112-116 |
| Number of pages | 5 |
| Journal | Australian Journal of Chemistry |
| Volume | 73 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Mar 2020 |
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