EC |
1.1.1.406 |
Accepted name: |
galactitol 2-dehydrogenase (L-tagatose-forming) |
Reaction: |
galactitol + NAD+ = L-tagatose + NADH + H+ |
Other name(s): |
GatDH |
Systematic name: |
galactitol:NAD+ 2-oxidoreductase (L-tagatose-forming) |
Comments: |
The enzyme, characterized in the bacterium Rhodobacter sphaeroides, has a wide subtrate specificity. In addition to galactitol, it primarily oxidizes D-threitol and xylitol, and in addition to L-tagatose, it primarily reduces L-erythrulose, D-ribulose and L-glyceraldehyde. It is specific for NAD+. The enzyme also shows activity with D-tagatose (cf. EC 1.1.1.16, galactitol 2-dehydrogenase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Schneider, K.H., Jakel, G., Hoffmann, R. and Giffhorn, F. Enzyme evolution in Rhodobacter sphaeroides: selection of a mutant expressing a new galactitol dehydrogenase and biochemical characterization of the enzyme. Microbiology 141 (1995) 1865–1873. [DOI] [PMID: 7551050] |
2. |
Carius, Y., Christian, H., Faust, A., Zander, U., Klink, B.U., Kornberger, P., Kohring, G.W., Giffhorn, F. and Scheidig, A.J. Structural insight into substrate differentiation of the sugar-metabolizing enzyme galactitol dehydrogenase from Rhodobacter sphaeroides D. J. Biol. Chem. 285 (2010) 20006–20014. [DOI] [PMID: 20410293] |
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[EC 1.1.1.406 created 2017] |
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