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Galactosylation Thermodynamics of E. Coli Beta-Galactosidase by Onpg and Pnpg

[ Vol. 8 , Issue. 4 ]


Jesse Oakes, Christain Castro and B. Mark Britt   Pages 303 - 306 ( 4 )


Michaelis-Menten analysis of the hydrolyses of ONPG and PNPG by E. coli beta-galactosidase were performed from 5.5 to 45 degree C. Analysis of the T-dependence of KM and kcat reveals the thermodynamics for formation of the E / S complex and attainment of the galactosylation transition state, respectively. While the binding and transition state free energies are similar for each substrate, the enthalpic and entropic contributions are found to differ substantially.


GALACTOSYLATION, E. COLI, GALACTOSIDASE, ONPG, PNPG, nitrophenyl galactopyranoside (ONPG), nitrophenyl galactopyranoside (PNPG)


Department of Chemistry and Biochemistry, P.O.Box 97348, Baylor University, Waco, TX 76798 USA

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