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

Authors: Oakes J.; Castro C.; Britt B.Mark

Source: Protein and Peptide Letters, Volume 8, Number 4, August 2001 , pp. 303-306(5)

Publisher: Bentham Science Publishers

Key:

- Free Content

- New Content

- Subscribed Content

- Free Trial Content

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)

Language: English

Document Type: Review article

DOI: 10.2174/0929866013409427

The full text electronic article is available for purchase. You will be able to download the full text electronic article after payment.

$55.10 plus tax Refund Policy