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Gene Review

ECs3370  -  inosine 5'-monophosphate dehydrogenase

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of ECs3370

  • Here we describe the expression of recombinant C. parvum IMPDH in an Escherichia coli strain lacking the bacterial homolog [1].
  • Expression, purification, and characterization of inosine 5'-monophosphate dehydrogenase from Borrelia burgdorferi [2].
  • An IMPDH homolog has been cloned from Borrelia burgdorferi, the causative agent of Lyme disease (Margolis, N., Hogan, D., Tilly, K., and Rosa, P. A. (1994) J. Bacteriol. 176, 6427-6432) [2].
  • The gene of IMP dehydrogenase of Bacillus cereus ts-4, a temperature-sensitive mutant of B. cereus JCM 2152, was subcloned and its sequence was analyzed [3].
 

High impact information on ECs3370

  • The pronounced resistance of C. parvum IMPDH to mycophenolic acid inhibition is in strong agreement with its bacterial origin [1].
  • C. parvum relies on inosine 5'-monophosphate dehydrogenase (IMPDH) to produce guanine nucleotides and is highly susceptible to IMPDH inhibition [1].
  • These data suggest that the structure and dynamic properties of the NAD binding site of C. parvum IMPDH can be exploited to develop parasite-specific inhibitors [1].
  • Cryptosporidium parvum IMP dehydrogenase: identification of functional, structural, and dynamic properties that can be exploited for drug design [1].
  • IMPDH converts IMP to xanthosine 5'-monophosphate with concomitant conversion of NAD+ to NADH [2].
 

Chemical compound and disease context of ECs3370

 

Biological context of ECs3370

 

Associations of ECs3370 with chemical compounds

  • Inosine 5'-monophosphate dehydrogenase (IMPDH) is the rate-limiting enzyme in de novo guanine nucleotide biosynthesis [2].
  • The third mutant IMPDH contains two mutations, Phe465 --> Ser and Asp470 --> Gly [11].
  • IMPDH converts inosine 5'-monophosphate (IMP) to xanthosine 5'-monophosphate (XMP) with concomitant conversion of NAD+ to NADH [7].
  • Further, denaturation/renaturation of the EICARMP-inactivated enzyme did not restore enzyme activity, which indicates that EICARMP forms a covalent adduct with IMPDH [7].
  • (6) The IMP dehydrogenase polypeptide contains an internal segment of 123 amino acid residues that has no counterpart in GMP reductase and may represent an independent folding domain flanked by (alanine + glycine)-rich interdomain linkers [12].
 

Other interactions of ECs3370

 

Analytical, diagnostic and therapeutic context of ECs3370

References

  1. Cryptosporidium parvum IMP dehydrogenase: identification of functional, structural, and dynamic properties that can be exploited for drug design. Umejiego, N.N., Li, C., Riera, T., Hedstrom, L., Striepen, B. J. Biol. Chem. (2004) [Pubmed]
  2. Expression, purification, and characterization of inosine 5'-monophosphate dehydrogenase from Borrelia burgdorferi. Zhou, X., Cahoon, M., Rosa, P., Hedstrom, L. J. Biol. Chem. (1997) [Pubmed]
  3. Molecular cloning, overproduction and characterization of the Bacillus cereus IMP dehydrogenase. Kim, S.I., Miyamoto, T., Honjoh, K.I., Hio, M., Hatano, S. Biosci. Biotechnol. Biochem. (2000) [Pubmed]
  4. IMP dehydrogenase from Pneumocystis carinii as a potential drug target. O'Gara, M.J., Lee, C.H., Weinberg, G.A., Nott, J.M., Queener, S.F. Antimicrob. Agents Chemother. (1997) [Pubmed]
  5. Inhibition of IMPDH by mycophenolic acid: dissection of forward and reverse pathways using capillary electrophoresis. Fleming, M.A., Chambers, S.P., Connelly, P.R., Nimmesgern, E., Fox, T., Bruzzese, F.J., Hoe, S.T., Fulghum, J.R., Livingston, D.J., Stuver, C.M., Sintchak, M.D., Wilson, K.P., Thomson, J.A. Biochemistry (1996) [Pubmed]
  6. Inhibitors of inosinic acid dehydrogenase. 2-Substituted inosinic acids. Wong, C.G., Meyer, R.B. J. Med. Chem. (1984) [Pubmed]
  7. Inactivation of inosine 5'-monophosphate dehydrogenase by the antiviral agent 5-ethynyl-1-beta-D-ribofuranosylimidazole-4-carboxamide 5'-monophosphate. Wang, W., Papov, V.V., Minakawa, N., Matsuda, A., Biemann, K., Hedstrom, L. Biochemistry (1996) [Pubmed]
  8. Asp338 controls hydride transfer in Escherichia coli IMP dehydrogenase. Kerr, K.M., Digits, J.A., Kuperwasser, N., Hedstrom, L. Biochemistry (2000) [Pubmed]
  9. Nucleotide sequence of the guaB locus encoding IMP dehydrogenase of Escherichia coli K12. Tiedeman, A.A., Smith, J.M. Nucleic Acids Res. (1985) [Pubmed]
  10. IMP dehydrogenase: mechanism of action and inhibition. Hedstrom, L. Current medicinal chemistry. (1999) [Pubmed]
  11. Isolation and characterization of mycophenolic acid-resistant mutants of inosine-5'-monophosphate dehydrogenase. Farazi, T., Leichman, J., Harris, T., Cahoon, M., Hedstrom, L. J. Biol. Chem. (1997) [Pubmed]
  12. Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12. Andrews, S.C., Guest, J.R. Biochem. J. (1988) [Pubmed]
  13. Complementation in vitro between guaB mutants of Escherichia coli K12. Gilbert, H.J., Drabble, W.T. J. Gen. Microbiol. (1980) [Pubmed]
  14. Effect of unusual guanosine nucleotides on the activities of some Escherichia coli cellular enzymes. Pao, C.C., Dyess, B.T. Biochim. Biophys. Acta (1981) [Pubmed]
  15. Inosine 5'-monophosphate dehydrogenase of Escherichia coli. Purification by affinity chromatography, subunit structure and inhibition by guanosine 5'-monophosphate. Gilbert, H.J., Lowe, C.R., Drabble, W.T. Biochem. J. (1979) [Pubmed]
  16. Differential splicing of Pneumocystis carinii f. sp. carinii inosine 5'-monophosphate dehydrogenase pre-mRNA. Ye, D., Lee, C.H., Queener, S.F. Gene (2001) [Pubmed]
  17. Cloning, sequence analysis and expression of the group A streptococcal guaB gene encoding inosine monophosphate dehydrogenase. Ashbaugh, C.D., Wessels, M.R. Gene (1995) [Pubmed]
 
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