Human IMP dehydrogenase (IMPDH) catalyzes the NAD-dependent oxidation of IMP to XMP, making it a key component in the synthesis of guanine nucleotides. Two isoforms of the enzyme exit and these two forms share approximately 84% sequence identity. There is evidence that inhibitors of type II IMPDH are effective antiproliferative agents, and may be useful in controlling some forms on cancer. It has also been shown that inhibitors if IMPDH have immunosuppressive activity. Future efforts to understand and utilize the therapeutic benefits resulting from the inhibition of IMPDH activity would be greatly aided by obtaining the structure of this enzyme.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-23
Application #
6586632
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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