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                    BIOINFORMATICS COLLOQUIUM
               School of Computational Sciences
                    George Mason University
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        A Functional Proteomics of Homoserine Acylation

                         Dr. Tim Born
                   Department of Chemistry
                    George Mason University


                 Tuesday, November 8, 2005
                             4:30 pm
           Verizon Auditorium, Prince William Campus
ABSTRACT 
Homoserine occupies an important juncture in bacterial amino acid 
biosynthesis.  Acylation of this metabolite commits it to methionine 
and S-adenosylmethionine biosynthesis, while phosphorylation directs it 
to threonine and isoleucine biosynthesis.  Moreover, bacteria have 
evolved two distinct enzymes capable of homoserine acylation, with each 
bacterial species containing the gene for only of these 
acyltransferases.  In my lab we are interested in both the mechanism of 
acyltransfer to homoserine catalyzed by these enzymes and the 
functional proteomics of their distribution.  The long-term goals of 
this project are to evaluate these enzymes as potential antibiotic 
targets and to ultimately design specific inhibitors of each 
acyltransferase.   In this seminar I will discuss the basic chemical 
mechanisms of the two acyltransferasese and then describe recent 
results which suggest that functional assignments, based on DNA 
sequence analysis, may be incorrect for a significant number of these 
proteins.

BIOSKETCH
Dr. Timothy L. Born received his B.S. in Chemistry from Calvin College 
in 1990, during which time he studied protein stability in the lab of 
Dr. Terry Gray using T4 lysozyme as a model protein.  Having nothing 
better to do with his life as graduation approached, he decided to 
postpone reality and began a Ph.D. program in biochemistry at the Mayo 
Clinic in Rochester, MN.  Despite spending far too much time on the 
softball fields, volleyball courts, and broomball rinks of Rochester, 
he did manage to complete his graduate work, receiving his Ph.D. in 
1996 under the guidance of Dr. Frank Rusnak for his project titled 
“Investigations into the catalytic mechanism of calcineurin, a 
serine/threonine protein phosphatase”.  He then joined Dr. John 
Blanchard’s lab at Albert Einstein College of Medicine in the Bronx 
where he developed research projects characterizing enzymes involved in 
the methionine biosynthetic pathway.  More recently, he is with the 
Department of Chemistry and Biochemistry, at George Mason University. 
Dr. Born has established an externally funded laboratory research 
program based on his work in Dr. Blanchard’s lab and he has helped to 
establish a new academic program in biochemistry.  
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Refreshments are served at 4:00 pm. Find the schedule and directions at
http://www.binf.gmu.edu/colloq.html