William J. Lennarz

William Joseph Lennarz (September 28, 1934 – October 27, 2021) was a biochemist at Stony Brook University. He focused the majority of his research on biochemical processes in cells.

Early life and education William J. Lennarz was born in New York City on September 28, 1934. Lennarz studied chemistry and organic chemistry. After working as a postdoctoral researcher at Harvard, he developed an interest in biochemistry, before taking a role at Stony Brook University. Lennarz began his academic career at Penn State University as a chemical engineering major, but eventually changed his course of study to chemistry. After graduating from Penn State, Lennarz attended the University of Illinois to pursue a graduate degree in organic chemistry. While attending the University of Illinois, Lennarz researched the use of boronic acids as a potential cancer treatment. When a beam of neutrons is applied to boron, it is capable of emitting alpha particles that have the ability to kill cells. With this property in mind, Lennarz attempted to incorporate boronic acids into cancer cells to create a mechanism to selectively destroy tumor cells. While in graduate school, Lennarz developed an interest in biochemistry that lead him to pursue postdoc work under Konrad Bloch at Harvard. At Harvard, Lennarz worked on research pertaining to the biosynthesis of fatty acids in yeast. Through his work at Harvard, he was able to play a role in discovering acyl carrier protein, which is an enzyme in the fatty acid biosynthesis cycle. After leaving Harvard, Lennarz was employed at Johns Hopkins and the University of Texas Cancer Center before arriving at Stony Brook.

Notable work

Early work Before his tenure at Stony Brook, Lennarz was involved in some notable studies. Along with Luis Leloir, Robert Spiro, Edward Heath, Lennarz was able to determine the mechanism by which N-linked oligosaccharides are added to proteins in the endoplasmic reticulum. Lennarz and his lab mates discovered that these sugars are transferred as a group, and are synthesized from a dolichol-linked oligosaccharide with a conserved structure. They found the precursor for these molecules had the structure (Man)nGlcNAcB1,4 →GlcNAc-P-P-dolichol, and each precursor had at least five mannose residues. Additionally, they discovered that precursor molecules contain one to two glucose molecules, which was a surprising find. Up until this point, all N-linked oligosaccharides that had been characterized lacked glucose molecules. This lead the group to postulate that the oligosaccharide component of the precursor was modified by glycosidase enzymes before the glycoprotein could be considered mature. This work was very important in laying the foundation for later research that described the mechanism for the complete assembly glycoproteins in the endoplasmic reticulum. The C-terminal domain, which was found to bind mHR23B, was also analyzed by Lennarz and his team. They discovered that binding to mHR23B is likely what activates the C-terminal catalytic domain of PNGase. Binding of these two proteins was also found to govern the interaction between mHR23B and p97, another protein involved in the proteasome degradation pathway. The two binding proteins were also found to compete with each other to bind the PNGase, and a complex of all three proteins was found to be unable to form.

Death Lennarz died in Williamsburg, Virginia on October 27, 2021, at the age of 87.