New formulae for folding catalysts make them multi-purpose enzymes

Biotechnology and Bioengineering

Volumn 56, Issue 6, 1997, Pages 645-649

  Moutiez, Mireille ^a   Guthapfel, Régine ^a   Gueguen, Paul ^a   Quéméneur, Eric ^a  

^a DIF   (France)

Author keywords

Multi purpose enzymes; Prolyl isomerase; Protein disulfide isomerase; Protein folding catalysts

Indexed keywords

BIOREACTORS; OXIDATION; PROTEINS; SULFUR COMPOUNDS;

AGAROSE; BIOTINYLATION; DIMETHYLSULFOXIDE; PROPYL ISOMERASE; PROTEIN DISULFIDE ISOMERASE; PROTEIN FOLDING CATALYSTS;

ENZYME IMMOBILIZATION;

BIOTIN; DIMETHYL SULFOXIDE; ISOMERASE; PROLYL ISOMERASE; PROTEIN DISULFIDE ISOMERASE; THIOL; UNCLASSIFIED DRUG;

ARTICLE; BIOREACTOR; CATALYST; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; OXIDATION; PROTEIN FOLDING;

EID: 0342617521     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19971220)56:6<645::AID-BIT7>3.0.CO;2-N     Document Type: Article

References (26)

1. Buchner, J., Brinkmann, U., Pastan, I. 1992. Renaturation of a single chain immunotoxin facilitated by chaperones and PDI. Biotechnol. 10: 682-685.
2. Cai, H., Wang, C. C., Tsou, C. L. 1994. Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J. Biol. Chem. 269: 24550-24552.
3. Clubb, R. T., Ferguson, S. B., Walsh, C. T., Wagner, G. 1994. Three-dimensional structure of Escherichia coli periplasmic cyclophilin. Biochemistry 33: 2761-2772.
4. Cole, P. A. 1996. Chaperone-assisted protein expression. Structure 4: 239-242.
5. Datar, R. V., Cartwright, T., Rosen, C.-G. 1993. Process economics of animal cell and bacterial fermentations: A case study analysis of tissue plasminogen activator. Bio/technol. 11: 349-357.
6. DeBernardez-Clark, E., Georgiou, G. 1991. Inclusion bodies and recovery of proteins from the aggregated state, pp. 1-20. In: G. Georgiou, and E. DeBernardez-Clark (eds.), Protein refolding. American Chemical Society, Washington, DC.
7. Freedman, R. B., Hirst T. R., Tuite, M. F. 1994. Protein disufide isomerase: Building bridges in protein folding. Trends Biochem. Sci. 19: 331-336.
8. Freedman, R. B. 1995. Folding helpers and unhelpful folders. Current Biology 4: 933-935.
9. Georgiou, G., Valax, P. 1996. Expression of correctly folded proteins in Escherichia coli. Curr. Opin. Biotech. 7: 190-197.
10. Harrison, R. K., Stein, R. L. 1990. Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding proteins: Evidence for the existence of a family of distinct enzymes. Biochemistry 29: 3813-3816.
11. Li, W., Handschumacher, R. E. 1993. Specific interaction of the cyclophilin-cyclosporin complex with the B subunit of calcineurin. J. Biol. Chem. 268: 14040-14044.
12. Lilie, H., Lang, K., Rudolph, R., Buchner, J. 1993. Prolyl isomerase catalyze antibody folding in vitro. Prot. Sci. 2: 1490-1496.
13. Liu, J., Walsh, C. T. 1990. Peptidyl-prolyl cis-trans isomerase from Escherichia coli: A periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A. Proc. Natl. Acad. Sci. USA 87: 4028-4032.
14. Lyles M. M., Gilbert H. F. 1991. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer. Biochemistry. 30: 613-619.
15. Morjana N. A., Gilbert H. F. 1994. Catalysis of protein folding by agarose-immobilized Protein Disulfide Isomerase. Prot. Expr. Purif. 5: 144-148.
16. Noiva, R., Lennarz, W. J. 1992. Protein disulfide isomerase, a multifunctional protein resident in the lumen of the endoplasmic reticulum. J. Biol. Chem. 267: 3553-3556.
17. Primm, T. P., Walker, K. W., Gilbert, H. F. 1996. Facilitated protein aggregation. Effects of calcium on the chaperone ant anti-chaperone activity of protein disulfide isomerase. J. Biol. Chem. 271: 33664-33669.
18. Puig, A., Gilbert, H. F. 1994. Protein disulfide isomerase exhibits chaperone activity in the oxidative refolding of lysozyme. J. Biol. Chem. 269: 7764-7771.
19. Quan, H., Fan, G., Wang, C. C. 1995. Independence of the chaperone activity of protein isomerase from its thioredoxin-like active site. J. Biol. Chem. 270: 17078-17080.
20. Rudolph, R., Lilie, H. 1996. In vitro folding of inclusion body proteins. FASEB J. 10: 49-56.
21. Schmid, F. X., Mayr, L. M., Mücke, M., Schönbrunner, E. R. 1993. Prolyl isomerases: Role in protein folding. Adv. Prot. Chem. 44: 25-66.
22. Schönbrunner, E. R., Schmid, F. X. 1992. Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding. Proc. Natl. Acad. Sci. USA 89: 4510-4513.
23. Tam, J. P., Wu, C.-R., Liu, W., Zhang, J.-W. 1991. Disulfide bond formation in peptides by dimethyl sulfoxide, scope and applications. J. Am. Chem. Soc. 113: 6657-6662.
24. Vuori, K., Myllylä, R., Pihlajaniemi, T., Kivirikko, K. I. 1992. Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coll: The multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity. J. Biol. Chem. 267: 7211-7214.
25. Wall, J. G., Plückthun, A. 1995. Effects of overexpressing folding modulators on the in vivo folding of heterologous proteins in Escherichia coli. Curr. Opin. Biotech. 6: 507-516.
26. Wittrup, K. D. 1995. Disulfide bond formation and eukaryotic secretory productivity. Curr. Opin. Biotech. 6: 203-208.