Designed human serum hyaluronidase 1 variant, HYAL1ΔL, exhibits activity up to pH 5.9

Journal of Biological Chemistry

Volumn 284, Issue 29, 2009, Pages 19173-19177

  Reitinger, Stephan ^a,d   Müllegger, Johannes ^b   Greiderer, Brigitte ^a   Nielsen, Jens Erik ^c   Lepperdinger, Günter ^a  

^a ERICH SCHMID INSTITUTE OF MATERIALS SCIENCE   (Austria)

^b Zymeworks Inc   (Canada)

^c UNIVERSITY COLLEGE DUBLIN   (Ireland)

^d UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE CENTER; ACTIVE SITE; BINDING CLEFTS; CLOSE PROXIMITY; CONSERVED RESIDUES; CYSTEINE RESIDUES; DIVERSE SPECIES; DYNAMIC STRUCTURAL CHANGES; HUMAN SERUM; HYALURONAN; HYALURONAN-DEGRADATION; LOOP FORMATION; PH OPTIMA; SERINE RESIDUES; SUBSTRATE BINDING; SUBSTRATE HYDROLYSIS; TETRAPEPTIDE SEQUENCE;

AMINES; AMINO ACIDS; BODY FLUIDS; ORGANIC ACIDS; SUBSTRATES;

BINDING SITES;

CYSTEINE; GLYCINE; HYALURONIC ACID; HYALURONIDASE; HYALURONIDASE 1; RECOMBINANT ENZYME; SERINE; TETRAPEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYMATIC DEGRADATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; CATALYSIS; CATALYTIC DOMAIN; FEMALE; GENETIC VARIATION; HUMANS; HYALURONIC ACID; HYALURONOGLUCOSAMINIDASE; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTANT PROTEINS; OOCYTES; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; STATIC ELECTRICITY; XENOPUS LAEVIS;

EID: 67749095248     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C109.004358     Document Type: Article

References (35)

1. Lepperdinger, G., Fehrer, C., and Reitinger, S. (2004) in Chemistry and Biology of Hyaluronan (Hari, G., ed) pp. 71-82, Elsevier Science Publishers B.V., Amsterdam
2. Bairoch, A. (2000) Nucleic Acids Res. 28, 304-305
3. Kreil, G. (1995) Protein Sci. 4, 1666-1669
4. Henrissat, B., and Bairoch, A. (1996) Biochem. J. 316, 695-696
5. Lepperdinger, G., and Kreil, G. (2004) in Chemistry and Biology of Hyaluronan (Hari, G., ed) pp. 585-598, Elsevier Science Publishers B.V., Amsterdam
6. Menzel, E. J., and Farr, C. (1998) Cancer Lett. 131, 3-11
7. Marković-Housley, Z., Miglierini, G., Soldatova, L., Rizkallah, P. J., Müller, U., and Schirmer, T. (2000) Structure 8, 1025-1035
8. Skov, L. K., Seppälä, U., Coen, J. J., Crickmore, N., King, T. P., Monsalve, R., Kastrup, J. S., Spangfort, M. D., and Gajhede, M. (2006) Acta Crystallogr. D Biol. Crystallogr. 62, 595-604
9. Chao, K. L., Muthukumar, L., and Herzberg, O. (2007) Biochemistry 46, 6911-6920
10. Frost, G. I., Csóka, A. B., Wong, T., and Stern, R. (1997) Biochem. Biophys. Res. Commun. 236, 10-15
11. Lepperdinger, G., Müllegger, J., and Kreil, G. (2001) Matrix Biol. 20, 509-514
12. Reitinger, S., Müllegger, J., and Lepperdinger, G. (2001) FEBS Lett. 505, 213-216
13. Reitinger, S., Boroviak, T., Laschober, G. T., Fehrer, C., Müllegger, J., Lindner, H., and Lepperdinger, G. (2008) Protein Expr. Purif 57, 226-233
14. Gmachl, M., Sagan, S., Ketter, S., and Kreil, G. (1993) FEBS Lett. 336, 545-548
15. Oettl M., Hoechstetter, J., Asen, I., Bernhardt, G., and Buschauer, A. (2003) Eur. J. Pharm Sci. 18, 267-277
16. Nielsen, J. E. (2007) J. Mol. Graph Model 25, 691-699
17. Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006) Bioinformatics 22, 195-201
18. Guex, N., and Peitsch, M. C. (1997) Electrophoresis 18, 2714-2723
19. DeLano, W. (2002) PyMOL Release 0.99, DeLano Scientific LLC, Palo Alto, CA
20. Reitinger, S., Laschober, G. T., Fehrer, C., Greiderer, B., and Lepperdinger, G. (2007) Biochem. J. 401, 79-85
21. Nielsen, J. E., and Vriend, G. (2001) Proteins 43, 403-412
22. Jorgensen, W. L., and Tirado-Rives, J. (1988) J. Am. Chem. Soc. 110, 1657-1666
23. Nielsen, J. E., Andersen, K. V., Honig, B., Hooft, R. W., Klebe, G., Vriend, G., and Wade, R. C. (1999) Protein Eng. 12, 657-662
24. Nicholls, A., and Honig, B. (1991) J. Comput. Chem. 12, 435-445
25. Müllegger, J., Reitinger, S., and Lepperdinger, G. (2001) Anal. Biochem. 293, 291-293
26. Müllegger, J., and Lepperdinger, G. (2002) Mech. Dev. 111, 25-35
27. Vriend, G. (1990) J. Mol. Graph 8, 52-56
28. Csóka, A. B., Frost, G. I., Wong, T., and Stern, R. (1997) FEBS Lett. 417, 307-310
29. Cherr, G. N., Meyers, S. A., Yudin, A. I., VandeVoort, C. A., Myles, D. G., Primakoff, P., and Overstreet, J. W. (1996) Dev. Biol., 175, 142-153
30. Meyer, M. F., Kreil, G., and Aschauer, H. (1997) FEBS Lett. 413, 385-388
31. Podyma, K. A., Yamagata, S., Sakata, K., and Yamagata, T. (1997) Biochem. Biophys. Res. Commun. 241, 446-452
32. Natowicz, M. R., and Wang, Y. (1996) Clin. Chim. Acta 245, 1-6
33. Joshi, M. D., Sidhu, G., Nielsen, J. E., Brayer, G. D., Withers, S. G., and McIntosh, L. P. (2001) Biochemistry 40, 10115-10139
34. Søndergaard, C. R., McIntosh, L. P., Pollastri, G., and Nielsen, J. E. (2008) J. Mol. Biol. 376, 269-287
35. Nielsen, J. E., and McCammon, J. A. (2003) Protein Sci. 12, 313-326