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

The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate
The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate
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.
0003-2697
44-49
Bryant, P.
b25c6534-2db1-4843-8b14-fb72613b2be6
Kriek, M.
e01ddb12-38a7-4733-9e13-c0e5d9670cca
Wood, R.J.
6694b71e-a4ec-49fd-b2a4-644a7534f9f0
Roach, P.L.
ca94060c-4443-482b-af3e-979243488ba9
Bryant, P.
b25c6534-2db1-4843-8b14-fb72613b2be6
Kriek, M.
e01ddb12-38a7-4733-9e13-c0e5d9670cca
Wood, R.J.
6694b71e-a4ec-49fd-b2a4-644a7534f9f0
Roach, P.L.
ca94060c-4443-482b-af3e-979243488ba9

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).

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
ORCID for P.L. Roach: ORCID iD orcid.org/0000-0001-9880-2877

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Date deposited: 06 Mar 2007
Last modified: 03 Dec 2019 01:53

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Contributors

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

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