Tyrosine83 is essential for the activity of E-coli galactoside transacetylase

Radeghieri, A., Bonoli, M., Parmeggiani, F. ORCID: https://orcid.org/0000-0001-8548-1090 and Hochkoeppler, A. 2007. Tyrosine83 is essential for the activity of E-coli galactoside transacetylase. Biochimica Et Biophysica Acta-Proteins and Proteomics 1774 (2) , pp. 243-248. 10.1016/j.bbapap.2006.11.013

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Abstract

The gene (lacA) coding for Escherichia coli galactoside transacetylase was cloned into the pTrcHisB plasmid, and the corresponding hexahistidine-tagged enzyme was over-expressed and purified. The kinetic constants of the tagged protein were determined, yielding values in excellent agreement with previous observations reported for the natural enzyme. LacA Tyrosine83 was then substituted with a Valine: by comparing the K-m and k(cat) values observed for wild type and mutant enzymes using isopropyl-thio-beta-D-galactopyranoside or p-nitrophenyl-beta-D-galactopyranoside as substrates, Tyrosine83 was identified as an essential residue for the catalytic activity of E. coli galactoside transacetylase. (c) 2006 Elsevier B.V. All rights reserved.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Pharmacy
Last Modified:	14 Oct 2024 10:55
URI:	https://orca.cardiff.ac.uk/id/eprint/172223

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