| EC |
1.1.1.346 |
| Accepted name: |
2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming) |
| Reaction: |
2-dehydro-L-gulonate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+ |
| Glossary: |
2-dehydro-L-gulonate = 2-dehydro-L-idonate = 2-keto-L-gulonate |
| Other name(s): |
2,5-diketo-D-gluconate-reductase (ambiguous); YqhE reductase; dkgA (gene name); dkgB (gene name) |
| Systematic name: |
2-dehydro-D-gluconate:NADP+ 2-oxidoreductase (2-dehydro-L-gulonate-forming) |
| Comments: |
The enzyme is involved in ketogluconate metabolism, and catalyses the reaction in vivo in the reverse direction to that shown [1]. It is used in the commercial microbial production of ascorbate. cf. EC 1.1.1.274, 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming). |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Sonoyama, T. and Kobayashi, K. Purification and properties of two 2,5-diketo-D-gluconate reductases from a mutant strain derived from Corynebacterium sp. J Ferment Technol. 65 (1987) 311–317. |
| 2. |
Miller, J.V., Estell, D.A. and Lazarus, R.A. Purification and characterization of 2,5-diketo-D-gluconate reductase from Corynebacterium sp. J. Biol. Chem. 262 (1987) 9016–9020. [PMID: 3597405] |
| 3. |
Yum, D.Y., Lee, B.Y. and Pan, J.G. Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-gluconate reductases in Escherichia coli. Appl. Environ. Microbiol. 65 (1999) 3341–3346. [PMID: 10427017] |
| 4. |
Maremonti, M., Greco, G. and Wichmann, R. Characterisation of 2,5-diketo-D-gluconic acid reductase from Corynebacterium sp. Biotechnology Letters 18 (1996) 845–850. |
| 5. |
Khurana, S., Powers, D.B., Anderson, S. and Blaber, M. Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-Å resolution. Proc. Natl. Acad. Sci. USA 95 (1998) 6768–6773. [DOI] [PMID: 9618487] |
|
| [EC 1.1.1.346 created 2013] |
| |
|
| |
|
Printable version