Abstract
I reflect on my research on pyridoxal phosphate (PLP) enzymes over fifty-five years and on how I combined research with marriage and family. My Ph.D. research with Esmond E. Snell established one aspect of PLP enzyme mechanism. My postdoctoral work first with Hans L. Kornberg and then with Alton Meister characterized the structure and function of another PLP enzyme, l-aspartate β-decarboxylase. My independent research at the National Institutes of Health (NIH) since 1966 has focused on the bacterial tryptophan synthase α2β2 complex. The β subunit catalyzes a number of PLP-dependent reactions. We have characterized these reactions and the allosteric effects of the α subunit. We also used chemical modification to probe enzyme structure and function. Our crystallization of the tryptophan synthase α2β2 complex from Salmonella typhimurium led to the determination of the three-dimensional structure with Craig Hyde and David Davies at NIH in 1988. This landmark structure was the first structure of a multienzyme complex and the first structure revealing an intramolecular tunnel. The structure has provided a basis for exploring mechanisms of catalysis, channeling, and allosteric communication in the tryptophan synthase α2β2 complex. The structure serves as a model for many other multiprotein complexes that are important for biological processes in prokaryotes and eukaryotes.
Highlights
I attended the University of Texas in Austin (UT-Austin), where my father was an associate professor of English
I was fortunate to be offered an independent position in the Laboratory of Biochemical Pharmacology at the National Institute of Arthritis and Metabolic Diseases (NIAMD) of the National Institutes of Health (NIH) in 1966
Unit in the  reaction were increased by 30-fold by interaction with the ␣ subunit suggested that this would be a good system for investigating the specificity and control of the catalytic site of a pyridoxal phosphate (PLP) enzyme
Summary
I attended the University of Texas in Austin (UT-Austin), where my father was an associate professor of English. Irving Crawford and Charles Yanofsky had reported that E. coli tryptophan synthase is an enzyme complex consisting of two separable polypeptides, designated the ␣ subunit and the  subunit [6]. Unit in the  reaction were increased by 30-fold by interaction with the ␣ subunit suggested that this would be a good system for investigating the specificity and control of the catalytic site of a PLP enzyme.
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