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. The general phenylpropanoid pathway controls carbon flow into a number of downstream biosynthetic pathways, ultimately resulting in a multitude of biologically important natural products. Structural characterization of 4-Coumarate:CoA Ligase (4CL), the final, activating enzyme in this initial pathway, would greatly facilitate progress in a number of important genetic engineering projects. The success of these projects has beneficial implications for the production of novel medicinal natural products, the reduction of toxic waste generated by the paper industry in the process of lignin removal, and the amount of nutritional value extractable from forage crops by grazing livestock. The weak diffraction of 4CL crystals necessitates access to a synchrotron x-ray source for structural elucidation. Five additional phenylpropanoid biosynthetic enzymes (PAL/TAL, F3H, DFR, FLS, and ANS) have been acquired, and are also targeted for structural characterization during the course of this project. When combined with the several flavonoid biosynthetic enzymes already functionally and structurally characterized in our lab, these enzymes represent the minimum enzymatic arrays necessary to reconstitute the general phenylpropanoid, flavonoid, flavonol, and anthocyanin biosynthetic pathways, starting from (L) tyrosine, a product of primary metabolism.
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