• Title Professor of Biology; Director of Undergraduate Studies
  • Education PhD, University of California, 1981
  • Web Address http://www.bu.edu/aldolase/
  • Phone 617-353-5310
  • Area of Interest biochemistry, enzymology, molecular and human genetics of enzymes in sugar metabolism
  • CV

Current Research

Virtually all organisms contain the glycolytic enzyme fructose bisphosphate aldolase. Vertebrates have three distinguishable isoforms of the enzyme; aldolase A, B, and C. Each of these isozymes has different tissue distribution and catalytic properties appropriately for their roles in sugar metabolism. The aldolases have also been implicated in a number of moonlighting functions involved in cell motility, infection, insulin signaling, and endocytosis. It is the goal of the laboratory to understand the biochemical, evolutionary, and developmental mechanisms responsible for the distinguishing features of the various aldolases.

Structure and function of aldolases — The structural and functional details of this ancient and essential glycolytic enzyme are being investigated by structural analysis via x-ray crystallography and electron microscopy of the structures of the different isozymes complexed with substrate or inhibitor.

Characterization of the genetic defects in hereditary fructose intolerance (HFI) — Mutations in the aldolase B gene manifest themselves in HFI, a genetic disorder that can cause liver disease, coma, and death. It is especially problematic for newborn infants at the time they are weaned to fructose-containing foods. A mouse knock-out model is being used to study the disease and mutations from HFI patients of different ethnic groups are being determined.

Evolution of the aldolases — Current projects include the characterization of moonlighting functions that have evolved by oblating these functions with RNAi and mutant forms of the enzyme in tissue culture cells.

Selected Publications

  • Oppelt SA, Zhang W, Tolan DR (2017) Specific regions of the brain are capable of fructose metabolism. Brain Research, 1657, 312-322. PMCID: 28034722.
  • Oppelt SA, Coffee EM, Tolan DR (2015) Aldolase-B Deficiency in Mice Phenocopies Hereditary Fructose Intolerance in Humans. Molecular Genetics and Metabolism, 114, 445-450. PMCID: 25637246.
  • Coffee EM, Tolan DR (2014) Chapter 3: Gluconeogenesis, in Inborn Errors in Metabolism: From Neonatal Screening to Metabolic Pathways. Lee, B. & Scaglia, F., eds. (Oxford University Press, New York), 68-91 of 384p. [ISBN: 9780199797585]
  • Ritterson Lew C, Tolan DR (2013) Aldolase Sequesters WASP and Affects WASP/Arp2/3-Stimulated Actin Dynamics. Journal of Cellular Biochemistry, 114, 1928-1939.
  • Ritterson Lew C, Tolan DR (2012) Targeting of several glycolytic enzymes using RNA interference reveals aldolase affects cancer-cell proliferation through a non-glycolytic mechanism. Journal of Biological Chemistry, 287, 42554-42563.
  • Stopa JS, Tolan DR (2011) Stabilization of the predominant hereditary fructose intolerance causing aldolase variant (A149P) with zwitterionic osmolytes. Biochemistry, 50, 663-671.
  • Coffee EM, Tolan DR (2010) Mutations in the promoter region of the Aldolase B gene that cause Hereditary Fructose Intolerance are common among Hispanics and African-Americans. Journal of Inherited Metabolic Disease 33, 715-725.
  • Funari VA, Voevodski K, Leyfer D, Yerkes L, Cramer D, Tolan DR (2010) Quantitative gene-expression profiles in real time from expressed sequence tag databases. Gene Expression, 14, 321-336.

Courses Taught:

  • BI108 Introductory Biology II
  • BI 421 Biochemistry I
  • BI 527 Biochemistry Laboratory
  • MB 722 Advanced Biochemistry

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