International Thiamine (Vitamin B-1) Conference at Rutgers Newark

April 26, 2002

Thiamine (Vitamin B-1) researchers from around the world will convene at Rutgers-Newark for an "International Conference on Thiamine: Its Biochemistry and Structural Biology," May 18-21. Thiamine is a coenzyme that plays a vital role in carbohydrate metabolism within all cells of the human body, as well as in certain human metabolic disorders.

Frank Jordan, Board of Governors professor of chemistry at Rutgers-Newark, is co-chairing the conference. Jordan noted that the highlight of the conference will be the presentation of "high-resolution, three-dimensional structures of several of the thiamin diphosphate-dependent enzymes whose defects lead to specific human metabolic disorders."

The last international thiamine conference was convened in 1996 in Blaubeuren, Germany. Approximately 80-100 researchers from around the globe will present their research during the four-day meeting at Rutgers-Newark.

Vitamin B1, or thiamine, is converted by human cells to the coenzyme thiamin diphosphate, which together with cognate proteins, is a catalyst for carbohydrate metabolism, a process that converts food into energy. Deficiencies of thiamin diphosphate are implicated in a number of metabolic disorders such as human pyruvate dehydrogenase complex deficiency, a neurodegenerative disorder; primary biliary cirrhosis, a degenerative liver disease; maple syrup urine disease, a potentially fatal metabolic disorder; and Wernicke-Korsakoff syndrome, a disease affecting alchoholics.

New technologies available to scientists around the world are having a significant effect on research, Jordan noted. "With recent advances in X-ray crystallography and more powerful computers, scientists are able to view the 3-D structure of thiamin diphosphate in the active site of enzymes. This helps us explain the molecular origins of some human diseases and may eventually enable us to develop novel treatments or interventions based on structural understanding," Jordan continued. "The fact that genetic defects of only one enzyme are responsible for a disease makes future development of drugs and treatments for this disease very promising."

One of the diseases associated with deficiency of thiamine, pyruvate dehydrogenase complex deficiency, affects children whose symptoms include biochemical imbalances such as primary lactic acidosis. These children exhibit neurological defects and for most the disease is fatal. Conference co-chair Mulchand Patel, a biochemistry professor at State University of New York-Buffalo School of Medicine, is a major contributor to research on this disorder.

Another human disease related to pyruvate dehydrogenase complex deficiency is primary biliary cirrhosis, a slow chronic liver disease characterized by progressive destruction of the bile ducts. In addition, defects in an enzyme of the alpha-ketoacid dehydrogenase complexes can lead to maple syrup urine disease, a metabolic disorder characterized by sweet-smelling urine.

It is associated with neurological disorders and mental retardation. Another disorder created by thiamine deficiency often brought on by alcoholism or malnourishment is Wernicke-Korsakoff syndrome, an unusual form of amnesia that results from a brain disorder.

Jordan's research, carried out in collaboration with the University of Pittsburgh School of Medicine Professor William Furey, focuses on identifying the three-dimensional structure of the Escherichia coli version of the pyruvate dehydrogenase complex, the first structural analysis of an enzyme from a family of bacterial enzymes, many of them pathogenic. "The long-term goal of the Rutgers-Newark research is to develop novel interventions to treat diseases caused by pathogenic bacteria without harming the human enzyme," Jordan said.

For conference details, contact Jordan at 973-353-5470. Conference information is also available online at http://chemistry.rutgers.edu.
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Rutgers University

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