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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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 |
| Item ID: | 44399 |
| Date Deposited: | 06 Mar 2007 |
| Last Modified: | 01 Jun 2011 04:40 |
| Contributors: | Bryant, P. (Author) Kriek, M. (Author) Wood, R.J. (Author) Roach, P.L. (Author) |
| Date: | 2006 |
| Status: | Published |
| Contact Email Address: | plr2@soton.ac.uk |
| URI: | http://eprints.soton.ac.uk/id/eprint/44399 |
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