Data on a thermostable enzymatic one-pot reaction for the production of a high-value compound from l-arabinose
Maria Bawn,
Fabiana Subrizi,
Gary J. Lye,
Tom D. Sheppard,
Helen C. Hailes,
John M. Ward
Affiliations
Maria Bawn
The Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, University College London, Bernard Katz Building, London WC1E 6BT, UK
Fabiana Subrizi
Department of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, UK
Gary J. Lye
The Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, University College London, Bernard Katz Building, London WC1E 6BT, UK
Tom D. Sheppard
Department of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, UK
Helen C. Hailes
Department of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, UK
John M. Ward
The Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, University College London, Bernard Katz Building, London WC1E 6BT, UK; Corresponding author.
The dataset presented in this article is related to the research article entitled “One-pot, two-step transaminase and transketolase synthesis of l-gluco-heptulose from l-arabinose” (Bawn et al., 2018 in press) [1]. This article presents data on initial experiments that were carried out to investigate new thermostable transketolase (TK) activities with l-arabinose. Transaminase (TAm) sequences from an in-house library of thermophilic strains were analyzed to compare homologies to characterized TAms with desired activity. DNA and amino acid sequences are presented for all the enzymes investigated. Calibration curves for products of the TK and TAm reactions are also presented along with chromatographic analysis of the various one-pot reactions.
