期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 30, 期 2, 页码 -出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2019.126792
关键词
IMPDH; GuaB2; Covalent inhibitor; Mycobacterium thermoresistibile IMPDH; 6-Cl-purine ribotide
资金
- Bill and Melinda Gates Foundation
- FP7 European Project MM4TB [260872]
- Croucher Foundation
- Cambridge Commonwealth, European and International Trust
- Jack Brockhoff Foundation [JBF 4186]
- National Health and Medical Research Council of Australia [APP1072476]
- Department of Biochemistry, University of Melbourne
- Newton Fund RCUK-CONFAP Grant - Medical Research Council (MRC)
- Fundacao de Amparo a Pesquisa do Estado de Minas Gerais (FAPEMIG) [MR/M026302/1]
- MRC [MR/M026302/1] Funding Source: UKRI
Inosine-5'-monophosphate dehydrogenase (IMPDH) is a rate-limiting enzyme involved in nucleotide biosynthesis. Because of its critical role in purine biosynthesis, IMPDH is a drug design target for immunosuppressive, anticancer, antiviral and antimicrobial chemotherapy. In this study, we use mass spectrometry and X-ray crystallography to show that the inhibitor 6-Cl-purine ribotide forms a covalent adduct with the Cys-341 residue of Mycobacterium thermoresistibile IMPDH.
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