Ketosteroid isomerase provides further support for the idea that enzymes work by electrostatic preorganization

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 9, 2010, Pages 4075-4080

  Kamerlin, Shina C L ^a   Sharma, Pankaz K ^a   Chu, Zhen T ^a   Warshel, Arieh ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

Electrostatic reorganization; Empirical valence bond; Enzyme catalysis; Transition state analogue

Indexed keywords

EQUILENIN; STEROID DELTA ISOMERASE;

ARTICLE; CATALYSIS; ELECTRIC ACTIVITY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME STABILITY; MOLECULAR STABILITY; PKA; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; ROTATION;

BIOCATALYSIS; KETOSTEROIDS; STATIC ELECTRICITY; STEROID ISOMERASES;

EID: 77749239790     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0914579107     Document Type: Article

References (17)

1. Warshel A, et al. (2006) Electrostatic basis for enzyme catalysis. Chem Rev 106:3210-3235.
2. Kamerlin SCL, Warshel A (2010) At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins Struct Funct Bioinformat, in press.
3. Kraut DA, et al. (2006) Testing electrostatic complementarity in enzyme catalysis: Hydrogen bonding in the ketosteroid isomerase oxyanion hole. PLoS Biol 4:0501-0519.
4. Sigala PA, et al. (2008) Testing geometrical discrimination within an enzyme active site: Constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole. J Am Chem Soc 130:13696-13708.
5. Warshel A (1978) Energetics of enzyme catalysis. Proc Natl Acad Sci USA 75:5250-5254.
6. Schwans JP, Kraut DA, Herschlag D (2009) Determining the catalytic role of remote substrate binding interactons in ketosteroid isomerase. Proc Natl Acad Sci USA 106:14271-14275.
7. Sigala PA, Fafarman AT, Bogard PE, Boxer SG, Herschlag D (2007) Do ligand binding and solvent exclusion alter the electrostatic character within the oxyanion hole of an enzymatic active site? J Am Chem Soc 129:12104-12105.
8. Dewar MJ (1986) New ideas about enzyme reactions. Enzyme 36:8-20.
9. Warshel A, Sharma PK, Chu ZT, Aqvist J (2007) Electrostatic contributions to binding of transition state analogues can be very different from the corresponding contributions to catalysis: Phenolates binding to the oxyanion hole of ketosteroid isomerase. Biochemistry 46:1466-1476.
10. Feierberg I, Åqvist J (2002) The catalytic power of ketosteroid isomerase investigated by computer simulation. Biochemistry 41:15728-15735.
11. Petrounia IP, Blotny G, Pollack RM (2000) Binding of 2-naphthols to D38E mutants of 3-oxo-Delta(5)-steroid isomerase: Variation of ligand ionization state with the nature of the electrophilic component. Biochemistry 39:110-116.
12. 5-steroid isomerase using the D38E and D38N Mutants: The energetic basis for catalysis. Biochemistry 33:12172-12183.
13. Zeng B, Bounds PL, Steiner RF, Pollack R (1992) Nature of the intermediate in the 3-oxo-.DELTA.5-steroid reaction. Biochemistry 31:1521-1528.
14. Olsson MHM, Parson WW, Warshel A (2006) Dynamical contributions to enzyme catalysis: Critical tests of a popular hypothesis. Chem Rev 106:1737-1756.
15. Warshel A (1991) Computer Modeling of Chemical Reactions in Enzymes and Solutions (John Wiley & Sons, New York).
16. Lee FS, Chu ZT, Warshel A (1993) Microscopic and semimicroscopic calculations of electrostatic energies in proteins by the POLARIS and ENZYMIX programs. J Comp Chem 14:161-185.
17. Kraut DA, Sigala PA, Fenn TD, Herschlag D (2010) Dissecting the paradoxical effects of hydrogen bond mutations in the ketosteroid isomerase oxyanion hole. Proc Natl Acad Sci USA 107:1960-1965.