Abstract
Shikimate 5-dehydrogenase (EC 1.1.1.25) is an important enzyme of the aromatic amino acid biosynthesis pathway. The shikimate 5-dehydrogenase (SDH) gene from the hyperthermophile Archaeoglobus fulgidus was PCR cloned and over-expressed in E. coli. The resulting recombinant enzyme with a Mr of 27,000 was purified to homogeneity. The enzyme had a specific activity of 727 U/mg at 87°C, and exhibited KmS for shikimate and NADP+ of 0.17 ± 0.03 mM and 0.19 ±0.01, respectively. At 87°C, the half life of the SDH was 2 hours. At 60°C and a specific activity of 104 U/mg, the half life was 17 days. The combination of high stability and activity for this archaeal SDH may make it useful for industrial chiral synthesis.
| Original language | English |
|---|---|
| Pages (from-to) | 701-702 |
| Number of pages | 2 |
| Journal | Annual International Conference of the IEEE Engineering in Medicine and Biology - Proceedings |
| Volume | 1 |
| Publication status | Published - 2002 |
| Externally published | Yes |
| Event | Proceedings of the 2002 IEEE Engineering in Medicine and Biology 24th Annual Conference and the 2002 Fall Meeting of the Biomedical Engineering Society (BMES / EMBS) - Houston, TX, United States Duration: Oct 23 2002 → Oct 26 2002 |
ASJC Scopus Subject Areas
- Signal Processing
- Biomedical Engineering
- Computer Vision and Pattern Recognition
- Health Informatics
Keywords
- Archaea
- Archaeoglobus fulgidus
- Aromatic amino acid biosynthesis
- Shikimate 5-dehydrogenase