LAUSR

What can one say about Eddy Fischer that hasn't already been said? Not only was he a great scientist who started a whole new field of protein regulation, but also an urbane, cultured, multilingual European who was equally at home in the concert hall, on a tennis court, flying a small plane, and at a scientific meeting poster session. What follows are reminiscences of my interactions with Eddy over a span of 40 years. I first learned about Eddy Fischer the scientist when I was a graduate student in the Department of Biochemistry at the University of Cambridge in the mid-1960s. As a student, my college expected me to “supervise” firstand second-year undergraduates who were taking the Part I biochemistry course—two to three students at a time for an hour a week. In the third and final year of my PhD, I rented a room on the upper level balcony overlooking the coaching yard of the famous Eagle pub, where I tutored groups of students sitting on cushions on the floor of my tiny room. The Eagle is not only near the old Department of Biochemistry building on the Downing Street science site in the middle of Cambridge, where I worked, but also very close to the Cavendish Laboratory's MRC unit “hut,” where Francis Crick and Jim Watson worked. Francis and Jim often used to retreat to the Eagle for lunch, and it was there on February 28, 1953, that Crick reportedly told the assembled lunch crowd that they had discovered the secret of life! In 1962, when I took the Part I biochemistry course, one section focused on glycogen and glucose metabolism. We were taught that glycogen phosphorylase activity is stimulated by phosphorylation (see Figure 1), but there were no details and no mention of the scientists that had made this groundbreaking discovery! A few years later, when it was my task to review these lectures for my student supervisees, I was able to describe the experiments that Eddy Fischer and Ed Krebs had carried out between 1953 and 1959 that led to their seminal discovery that the activity of glycogen phosphorylase, the key enzyme that breaks down glycogen into glucose-1-phosphate, is stimulated by phosphorylase kinase-mediated phosphorylation of the less active phosphorylase b isoform at a single serine residue near its N-terminus, converting it into the highly active phosphorylase a isoform. I hope the students grasped the importance of this discovery, which was the first evidence that protein function can be regulated by addition of a phosphate group, but I suspect that most of them were only interested in passing the end of year exam! As everyone knows, Eddy's long-term interest in protein phosphorylation stemmed from the work he did with