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).

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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
Digital Object Identifier (DOI): doi:10.1016/j.ab.2006.01.023
ISSNs: 0003-2697 (print)
Subjects:
ePrint ID: 44399
Date :
Date Event
2006Published
Date Deposited: 06 Mar 2007
Last Modified: 16 Apr 2017 18:44
Further Information:Google Scholar
URI: http://eprints.soton.ac.uk/id/eprint/44399

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