CRYSTALLOGRAPHIC ANALYSIS OF LIGNIN BIOSYNTHETIC ENZYMES

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Lignins are phenolic polymers that are deposited in the secondary cell wall of plants, providing plants with such essential properties as structural support, resistance to biodegradation, and water transport. These polymers are derived from a diverse set of linkages of three chemically distinct monolignol precursors. An intensive structural investigation of monolignol biosynthetic enzymes, cinnamoyl-CoA reductase (CCR), coniferaldehyde alcohol dehydrogenase (CAD), and sinapaldehyde alcohol dehydrogenase (SAD), will reveal key details of enzymatic specificity crucial to lignin formation. In addition, knowledge gained from structural elucidation of these key enzymes will prove critical for a rational approach to engineering of the lignin biosynthetic pathway to synthesize novel monolignols. Due to the subtle chemical variations in substrates and products of this pathway, a synchrotron X-ray source will prove essential for determining high resolution structures necessary to reveal mechanistic details of monolignol biosynthesis.