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

Jesse      Oakes; Christain      Castro; B.   Mark   Britt

Abstract

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.

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

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Protein & Peptide Letters

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

Volume: 8 Issue: 4

Author(s): Jesse Oakes, Christain Castro and B. Mark Britt

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

Abstract: 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.

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Oakes Jesse, Castro Christain and Britt Mark B., Galactosylation Thermodynamics of E. Coli Beta-Galactosidase by Onpg and Pnpg, Protein & Peptide Letters 2001; 8 (4) . https://dx.doi.org/10.2174/0929866013409427