Here’s a salacious image from my little corner of the Garden State.
Just look at that yearning pistil and those turgid stamens. Ooooh, baby! Here’s the full shot of the flowers.
Part of my rather checkered undergrad majors included botany. My interest in plant physiology shoved me in the direction of biochemistry and organic chemistry, but I retain an affection for plants. These Casa Blanca lilies are just a few of the flowers gracing my deck.
My undergrad research project involved 1,3-beta-glucan synthase (EC 220.127.116.11) which I more or less isolated (please don’t ask me about protein purity) from Lilium longiflorum pollen. This enzyme uses UDP-glucose as a substrate with beta-linked di- and trisaccharides as templates. Beta-1,3-glucan is a well established permeability barrier, and abundant in pollen cell walls. Its better known cousin, beta-1,4-glucan, is known as cellulose. Beta-1,3-glucan is the major component of fungal cell walls, and thus, the corresponding glucan synthase is a target for antifungal therapy.
Harvesting the pollen from the trumpet lilies in the horticulture greenhouses was marvelous. Tissue collection from fragrant flowers certainly was more pleasing than rooting around a still warm bovine abdominal cavity in search of adrenal glands. Back in the day, isolation and purification of plant enzymes were buggerly difficult. Plant cells yielded their contents grudgingly, and guarded them behind formidable cell walls. Hence, prior to these latter years of recombinant proteins, advances in mechanistic enzymology came primarily from mammalian metabolic enzymes. We joked about “The world’s most overworked enzymes” and included liver alcohol dehydrogenase among these. Of course,, “overworked” has multiple implications for this particular protein!