P1-S1 interactions control the enantioselectivity and hydrolytic activity of the norleucine phenylesterase catalytic antibody 17E8

Journal of the American Chemical Society

Volumn 118, Issue 27, 1996, Pages 6510-6511

  Wade, Herschel ^a   Scanlan, Thomas S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; ESTERASE;

ARTICLE; CHIRALITY; ENZYME ACTIVITY; ENZYME BINDING;

EID: 0029949258     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9605329     Document Type: Article

References (12)

1. Guo, J.; Huang, W.; Scanlan, T. S. J. Am. Chem. Soc. 1994, 116, 6062.
2. Zhou, G. W.; Guo, J.; Huang, W.; Fletterick, R. J.; Scanlan, T. S. Science 1994, 265, 1059.
3. Castro, B.; Evin, G.; Selve, C.; Seyer, R. Synthesis 1977, 413. Both the R and S enantiomers of the norleucine (2) and alanine (3) were prepared by this route. The α-amino isobutyric acid (Aib, 4) and glycine (5) substrates, which are nonstereogenic at Ca, were prepared by direct esterifrcation of the corresponding N-formyl amino acid. Phenyl hexanoate, a substrate that possesses the n-butyl P1 side chain but does not contain the α-formylamino substituent, was: prepared by esterification of hexanoic acid.
4. M were obtained from a nonlinear fit of the υ vs [S] data to the Michaelis - Menten equation using the Kaleidagraph program.
5. Stroud, R. M. Sci. Am. 1974, 231, 74.
6. Ingles, D. W.; Knowles, J. R. Biochem. J. 1967, 104, 369.
7. Ingles, D. W.; Knowles, J. R. Biochem. J. 1968, 108, 561.
8. M values between the (S)-3 and racemic 3 substrates is not as apparent as with the natural norleucine substrate 2.
9. Berezin, I. V.; Kazanskaya, N. F.; Klyosov, A. A. FEBS Lett. 1971, 15, 121.
10. M) vs the hydrophobicity constant π shows a linear correlation for the series including the Phe data. Dorovskaya, S.; Varfolomeyev, D.; Kazanskaya, N. F.; Klyosov, A. A.; Martinek, K. FEBS Lett. 1972, 23, 122.
11. Perona, J. J.; Craik, C. S. Protein Sci. 1995, 4, 337-360.
12. Fersht, A. Enzyme Structure and Mechanism, 2nd ed.; W. H. Freeman & Co.: New York, 1985; p 350.