| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1178018 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2011 | 14 Pages |
PLP is well-regarded for its role as a coenzyme in a number of diverse enzymatic reactions. Transamination, deoxygenation, and aldol reactions mediated by PLP-dependent enzymes enliven and enrich deoxy sugar biosynthesis, endowing these compounds with unique structures and contributing to their roles as determinants of biological activity in many natural products. The importance of deoxy aminosugars in natural product biosynthesis has spurred several recent structural investigations of sugar aminotransferases. The structure of a PMP-dependent enzyme catalyzing the C-3 deoxygenation reaction in the biosynthesis of ascarylose was also determined. These studies, and the crystal structures they have provided, offer a wealth of new insights regarding the enzymology of PLP/PMP-dependent enzymes in deoxy sugar biosynthesis. In this review, we consider these recent achievements in the structural biology of deoxy sugar biosynthetic enzymes and the important implications they hold for understanding enzyme catalysis and natural product biosynthesis in general. This article is part of a Special Issue entitled: Pyridoxal Phosphate Enzymology.
Graphical AbstractFigure optionsDownload full-size imageDownload high-quality image (148 K)Download as PowerPoint slideResearch Highlights► A survey of PLP-dependent enzymes in prokaryotic deoxy aminosugar biosynthesis. ► Catalysis in the context of recent aminotransferase/dehydratase structural studies. ► Focus on deoxy aminosugars decorating prokaryotic natural products.
