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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), pp. 44-49. (doi:10.1016/j.ab.2006.01.023).

Record type: Article

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.

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Published date: 2006

Identifiers

Local EPrints ID: 44399
URI: http://eprints.soton.ac.uk/id/eprint/44399
ISSN: 0003-2697
PURE UUID: 80351c92-b910-4e7e-b6d5-a8cc3518de30

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Date deposited: 06 Mar 2007
Last modified: 17 Jul 2017 15:14

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Contributors

Author: P. Bryant
Author: M. Kriek
Author: R.J. Wood
Author: P.L. Roach

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