Specific biotinylation of IMP dehydrogenase

IMP dehydrogenase (IMPDH) catalyzes a critical step in guanine nucleotide biosynthesis. IMPDH also has biological roles that are distinct from its enzymatic function. We report a biotin-linked reagent that selectively labels IMPDH and is released by dithiothreitol. This reagent will be invaluable in...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 2011-03, Vol.21 (5), p.1363-1365
Main Authors: Hoefler, B. Christopher, Gollapalli, Deviprasad R., Hedstrom, Lizbeth
Format: Article
Language:English
Subjects:
6-Cl-purine ribotide
Analytical, structural and metabolic biochemistry
Biological and medical sciences
biosynthesis
Biotin probe
Biotinylation
dithiothreitol
Dithiothreitol - chemistry
Enzyme inhibitors
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
guanine nucleotides
Humans
IMP Dehydrogenase - chemistry
IMPDH
inosine monophosphate
Mechanism-based probe
Models, Molecular
Molecular Structure
Nucleotide biosynthesis
Oxidoreductases
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Summary:IMP dehydrogenase (IMPDH) catalyzes a critical step in guanine nucleotide biosynthesis. IMPDH also has biological roles that are distinct from its enzymatic function. We report a biotin-linked reagent that selectively labels IMPDH and is released by dithiothreitol. This reagent will be invaluable in elucidating the moonlighting functions of IMPDH.
ISSN:0960-894X
1464-3405
DOI:10.1016/j.bmcl.2011.01.042