Function
Inosine monophosphate dehydrogenase (IMPDH) is part of the GTP biosynthesis and catalyzes the conversion of inosine monophosphate to xanthosine monophosphate while reducing NAD. IMPDH is inhibited by ribavirin and mycophenolic acid.
Disease
Relevance
Structural highlights
3D structures of inosine monophosphate dehydrogenase
Updated on 28-August-2014
IMPDH
1ak5 – TfIMPDH – Tritrichomonas foetus
1eep – IMPDH – Borellia burgdorferi
1zfj – IMPDH catalytic domain – Streptococcus pyogenes
1vrd – IMPDH – Thermotoga maritima
3ffs – CpIMPDH – Cryptosporidium parvum
3r2g – IMPDH – Legionella pneumophila
3tsb, 4mjm – BaIMPDH (mutant) – Bacillus anthracis
4fez – VcIMPDH – Vibrio cholerae
4avf, 3zfh – PaIMPDH – Pseudomonas aeruginosa
IMPDH binary complex
1me8 – TfIMPDH + ribavirin monophosphate
1pvn – TfIMPDH catalytic domain + transition state analog
1me9 – TfIMPDH + inosinic acid
2cu0 – IMPDH + xanthosine monophosphate – Pyrococcus horikoshii
3tsd – BaIMPDH (mutant) + xanthosine monophosphate
3usb – BaIMPDH + inosinic acid
4ix2 – VcIMPDH + inosinic acid
4dqw – PaIMPDH + ATP
IMPDH ternary complex
1me7 – TfIMPDH + ribavirin monophosphate + mycophenolic acid
1lrt – TfIMPDH + adenine derivative + inosinic acid
1meh – TfIMPDH + mycophenolic acid + inosinic acid
1mei – TfIMPDH + mycophenolic acid + xanthosine monophosphate
1mew – TfIMPDH + NAD + xanthosine monophosphate
3khj – CpIMPDH + inhibitor + inosinic acid
4fo4, 4fxs – VcIMPDH + mycophenolic acid + inosinic acid
4hlv – VcIMPDH + NAD + inosinic acid
4ixh – CpIMPDH catalytic domain + benzoxazole inhibitor + inosinic acid
4my8 – BaIMPDH catalytic domain (mutant) + benzoxazole inhibitor + inosinic acid
4my1, 4mya, 4mxs, 4my9 – BaIMPDH catalytic domain (mutant) + inhibitor + inosinic acid
4mz1 – IMPDH catalytic domain (mutant) + inhibitor + inosinic acid – Campylobacter jejuni
4af0 – IMPDH + mycophenolic acid + inosinic acid – Cryptococcus neoformans
References
