Protein engineering the surface of enzymes

Journal of Biotechnology

Volumn 66, Issue 1, 1998, Pages 11-26

  Petersen, Steffen B ^a   Harald Jonson, Per ^a   Fojan, Peter ^a   Petersen, Evamaria I ^a   Neves Petersen, Maria Teresa ^a   Hansen, Sissel ^b   Ishak, Rodney J ^b   Hough, Edward ^b  

^a AALBORG UNIVERSITY   (Denmark)

^b UNIVERSITY OF TROMSØ   (Norway)

Author keywords

Cutinase; Entropy stabilisation; Microcalorimetry; Protein electrostatics; Protein engineering; Protein stability; Protein surface

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; DIFFERENTIAL SCANNING CALORIMETRY; ELECTROSTATICS; ENTROPY; HYDROPHOBICITY; PH EFFECTS; SOLVENTS; SURFACE STRUCTURE; X RAY DIFFRACTION ANALYSIS;

CUTINASE; DEPROTONATION; PROTEIN ENGINEERING;

ENZYMES;

CUTINASE; PROTEIN;

AMINO ACID SEQUENCE; BIOTECHNOLOGY; CONFERENCE PAPER; ELECTRICITY; ENTHALPY; ENZYME ACTIVITY; GENETIC ENGINEERING; MOLECULE; PRIORITY JOURNAL; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION; SURFACE PROPERTY; THERMOSTABILITY; X RAY DIFFRACTION;

BINDING SITES; CARBOXYLIC ESTER HYDROLASES; DATABASES, FACTUAL; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEINS; RECOMBINANT PROTEINS; SOLVENTS;

EID: 0344878863     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(98)00153-9     Document Type: Conference Paper

References (25)

1. Anthonsen H.W., Baptista A., Drabløs F., Martel P., Petersen S.B. The blind watchmaker and rational protein engineering. J. Biotechnol. 36:1994;185-220.
2. Brünger, A.T., 1992. X-PLOR, version 3.1: a system for X-ray crystallography and NMR. Yale University Press, New Haven, CT.
3. Chothia C. Structural invariants in protein folding. Nature. 254:1975;304-308.
4. Chothia C. The nature of the accessible and buried surfaces in proteins. J. Mol. Biol. 105:1976;1-14.
5. Colloborative Computational Project, Number 4, 1994. The CCP4 suite: programs for protein crystallography. Acta Cryst. D50, 760-763.
6. Go M., Miyazawa S. Relationship between mutability, polarity and exteriority of amino acid residues in protein evolution. Int. J. Pept. Protein Res. 15:1980;211-224.
7. Grantham R. Amino acid difference formula to help explain protein evolution. Science. 185:1974;862-864.
8. Hobohm U., Sander C. Enlarged representative set of protein structures. Protein Sci. 3:1994;522-524.
9. Janin J. Surface and inside volumes in globular proteins. Nature. 277:1979;491-492.
10. Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
11. Koshi J.M., Goldstein R.A. Context-dependent optimal substitution matrices. Protein Eng. 8:1995;641-645.
12. Lauwereys, M., de Geus, P., de Meutter, J., Stanssens, P., Matthyssens, G., 1990. Cloning, expression and characterization of cutinase, a fungal lipolytic enzyme. In: Alberghina, L., Schmid, R.D., Verger, R. (Eds.), Lipases: Structure, Mechanism and Genetic Engineering. Verlag Chemie, Weinheim.
13. Lee B., Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:1971;379-400.
14. Longhi S., Nicolas A., Creveld L., Egmond M., Verrips C.T., de Vlieg J., Martinez C., Cambillau C. Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants. Proteins. 26:1996;442-458.
15. Longhi S., Mannesse M., Verheij H.M. et al. Crystal structure of cutinase covalently inhibited by a triglyceride analouge. Protein Sci. 6:1997;275-286.
16. Martel P.J., Baptista A., Petersen S.B. Protein electrostatics. Biotechnol. Ann. Rev. 2:1996;315-372.
17. Martinez C., De Geus P., Lauwereys M., Matthyssens G., Cambillau C. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature. 356:1992;615-618.
18. Miller S., Janin J., Lesk A.M., Chothia C. Interior and surface of monomeric proteins. J. Mol. Biol. 196:1987;641-656.
19. Navaza J. AMoRe-an automated package for molecular replacement. Acta Cryst. A50:1994;157-163.
20. Nicholls A., Sharp K., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
21. Otwinowski, Z., 1993. Oscillation data reduction program. In: Sawyer, L., Issacs, N., Bailey, S. (Eds.), Data Collection and Processing. SERC Daresbury Laboratory, Warrington, UK, pp. 56-62.
22. Plotnikov V.V., Brandts J.M., Lin L.N., Brandts J.F. A new ultrasensitive scanning calorimeter. Anal. Biochem. 250:1997;237-244.
23. Sander C., Schneider R. Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins. 9:1991;56-68.
24. Sanchez-Ruiz J.M., Lopez-Lacomba J.L., Cortijo M., Mateo P.L. Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry. 27:1988;1648-1652.
25. Studier F.W., Rosenberg A.H., Dunn J.J., Dubendorff J.W. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185:1990;60-89.