The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate


Bryant, P., Kriek, M., Wood, R.J. and Roach, P.L. (2006) The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate. Analytical Biochemistry, 351, (1), 44-49. (doi:10.1016/j.ab.2006.01.023).

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Original Publication URL: http://dx.doi.org/10.1016/j.ab.2006.01.023

Description/Abstract

The protein lipoyl synthase (LipA) is essential for lipoic acid biosynthesis via sulfur insertions into a protein-bound octanoyl group. We have developed an in vitro assay for LipA using a synthetic tetrapeptide Substrate, containing an N-epsilon-octanoyl lysine residue, corresponding in sequence to the lipoyl binding domain of the E2 subunit of pyruvate dehydrogenase. A putative LipA from the hypothermophilic archaea Sulfolobus solfataricus was expressed in Escherichia coli and purified, and the activity was measured using this novel assay. The optimal temperature for the S. solfataricus LipA-dependent formation of the lipoyl group was found to be 60 degrees C.

Item Type: Article
ISSNs: 0003-2697 (print)
Related URLs:
Subjects: Q Science
Q Science > QD Chemistry
Divisions: University Structure - Pre August 2011 > School of Chemistry
ePrint ID: 44399
Date Deposited: 06 Mar 2007
Last Modified: 27 Mar 2014 18:28
Contact Email Address: plr2@soton.ac.uk
URI: http://eprints.soton.ac.uk/id/eprint/44399

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