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Gene Review

Y17G9B.4  -  Protein Y17G9B.4

Caenorhabditis elegans

 
 
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Disease relevance of isomerase

  • Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit [1].
 

High impact information on isomerase

  • This enzyme is required for the proper maintenance of post-embryonic body shape in strains with a weakened cuticle, perhaps through ECM stabilization via cross-linking activity, disulfide isomerase protein folding activity, protein disulfide isomerase chaperone activity, or via multifunctional events [2].
  • The peptidyl-prolyl isomerase activity of CYP-3 has been characterized against the substrate N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, and gives a k(cat)/K(m) value of 2.4 x 10(6) M(-1) s(-1) [3].
  • Cyclophilin is identical with peptidylprolyl cis-trans isomerase (PPI; EC 5.2.1.8), an enzyme which catalyses the isomerization between the two proline conformations in proteins, thereby acting as a catalyst in protein-folding events [4].
  • Screening of cDNA libraries with polyclonal antibodies raised against L4Pepst and AdPepst showed that a protein disulphide isomerase (Ost-PDI2) was present in both antigen fractions [5].
  • This cDNA contains a single, long open reading frame that encodes sequence motifs identical to the two known active sites of PDI for isomerase activity [6].
 

Associations of isomerase with chemical compounds

 

Other interactions of isomerase

  • Transglutaminases, thioredoxins and protein disulphide isomerase: diverse enzymes with a common goal of cross-linking proteins in lower organisms [10].

References

  1. Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit. Veijola, J., Annunen, P., Koivunen, P., Page, A.P., Pihlajaniemi, T., Kivirikko, K.I. Biochem. J. (1996) [Pubmed]
  2. The Caenorhabditis elegans ERp60 homolog protein disulfide isomerase-3 has disulfide isomerase and transglutaminase-like cross-linking activity and is involved in the maintenance of body morphology. Eschenlauer, S.C., Page, A.P. J. Biol. Chem. (2003) [Pubmed]
  3. Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans. Dornan, J., Page, A.P., Taylor, P., Wu, S., Winter, A.D., Husi, H., Walkinshaw, M.D. J. Biol. Chem. (1999) [Pubmed]
  4. Cloning and biochemical characterization of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans. Page, A.P., MacNiven, K., Hengartner, M.O. Biochem. J. (1996) [Pubmed]
  5. Protein disulphide isomerase of Ostertagia ostertagi: an excretory-secretory product of L4 and adult worms? Geldhof, P., Vercauteren, I., Knox, D., Demaere, V., Van Zeveren, A., Berx, G., Vercruysse, J., Claerebout, E. Int. J. Parasitol. (2003) [Pubmed]
  6. The Onchocerca volvulus homologue of the multifunctional polypeptide protein disulfide isomerase. Wilson, W.R., Tuan, R.S., Shepley, K.J., Freedman, D.O., Greene, B.M., Awadzi, K., Unnasch, T.R. Mol. Biochem. Parasitol. (1994) [Pubmed]
  7. Novel nuclear methylation of sterols by the nematode Caenorhabditis elegans. Chitwood, D.J., Lusby, W.R., Lozano, R., Thompson, M.J., Svoboda, J.A. Steroids (1983) [Pubmed]
  8. Molecular and biochemical characterization of a protein cyclophilin from the nematode Haemonchus contortus( P ). Valle, C., Troiani, A.R., Lazzaretti, P., Bouvier, J., Cioli, D., Klinkert, M.Q. Parasitol. Res. (2005) [Pubmed]
  9. Structural elements responsible for transglutaminase activity of protein disulphide isomerases and thioredoxins. Blaskó, B., Mádi, A., Fésüs, L. J. Biol. Regul. Homeost. Agents (2004) [Pubmed]
  10. Transglutaminases, thioredoxins and protein disulphide isomerase: diverse enzymes with a common goal of cross-linking proteins in lower organisms. Rao, R.U., Mehta, K. Indian J. Exp. Biol. (2004) [Pubmed]
 
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