The crystal structure of the catalytic domain of tyrosine hydroxylase (TyrOH) to 2.3 E resolution has recently been completed in our laboratory by the MIRAS method. Structural studies are in progress of TyrOH with substrates, inhibitors, and the required biopterin cofactor bound. Using molecular replacement with TyrOH, structural studies have begun for the closely related enzyme phenylalanine hydroxylase. These high resolution structures will provide new knowledge about the function of this family of enzymes as well as the role of single amino acid mutations that cause human diseases such as L-DOPA responsive parkinsonism and phenylketonuria (PKU).

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-23
Application #
6586658
Study Section
Project Start
2002-03-01
Project End
2003-02-28
Budget Start
Budget End
Support Year
23
Fiscal Year
2002
Total Cost
$143,176
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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