Holden

Hazel M Holden

           

Professor,
A.B., Duke University;
Ph.D., Washington University

      

Three-dimensional structures of proteins by x-ray crystallographic analysis

Knowledge of the molecular structure of an enzyme is critically important in understanding its function, and x-ray crystallography is, to date, the most powerful technique available for obtaining such information.  Research interest in this laboratory focuses on enzymes involved in carbohydrate metabolism.

The biological importance of carbohydrates cannot be overstated for they are essential elements in nearly every physiological process and represent the most abundant biomolecules in living systems.  Apart from their role in providing metabolic energy, carbohydrates are involved in a wide range of biological processes including the immune response, cell-cell interactions, fertilization, and cell adhesion, among others.  Presently we are continuing our x-ray structural and biochemical analyses of the four enzymes that constitute the Leloir pathway for normal galactose metabolism.  Defects in the genes encoding these enzymes can lead to the diseased state referred to collectively as galactosemia.  We have also initiated structural studies on the proteins in Saccharomyces cerevisiae that regulate transcription of the genes the encode these four enzymes.

Another area of research interest is in the structure and function of enzymes involved in the synthesis of the unusual deoxysugars, tyvelose and desosamine.  Tyvelose is a 3,6-dideoxyhexose that occurs in the O-antigens of some Gram-negative bacteria and has been speculated to play a role in the pathogenicity of these organisms.  Desosamine is a 3-amino-3,4,6-trideoxyhexose found in certain macrolide antibiotics such as the commonly prescribed erythromycin.  The addition of unusual deoxysugars such as D-desosamine to such polyketide antibiotics provides or enhances their biological activity.



    

 

 

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