| EC |
4.2.1.46 |
| Accepted name: |
dTDP-glucose 4,6-dehydratase |
| Reaction: |
dTDP-α-D-glucose = dTDP-4-dehydro-6-deoxy-α-D-glucose + H2O |
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For diagram of 6-deoxyhexose biosynthesis, click here |
| Other name(s): |
thymidine diphosphoglucose oxidoreductase; TDP-glucose oxidoreductase; dTDP-glucose 4,6-hydro-lyase; dTDP-glucose 4,6-hydro-lyase (dTDP-4-dehydro-6-deoxy-α-D-glucose-forming) |
| Systematic name: |
dTDP-α-D-glucose 4,6-hydro-lyase (dTDP-4-dehydro-6-deoxy-α-D-glucose-forming) |
| Comments: |
Requires bound NAD+. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37259-54-4 |
| References: |
| 1. |
Gilbert, J.M., Matsuhashi, M. and Strominger, J.L. Thymidine diphosphate 4-acetamido-4,6-dideoxyhexoses. II. Purification and properties of thymidine diphosphate D-glucose oxidoreductase. J. Biol. Chem. 240 (1965) 1305–1308. [PMID: 14284740] |
| 2. |
Melo, A., Elliott, H. and Glaser, L. The mechanism of 6-deoxyhexose synthesis. I. Intramolecular hydrogen transfer catalyzed by deoxythymidine diphosphate D-glucose oxidoreductase. J. Biol. Chem. 243 (1968) 1467–1474. [PMID: 4869560] |
| 3. |
Wang, S.-F. and Gabriel, O. Biological mechanisms involved in the formation of deoxy sugars. V. Isolation and crystallization of thymidine diphosphate-D-glucose oxidoreductase from Escherichia coli B. J. Biol. Chem. 244 (1969) 3430–3437. [PMID: 4307450] |
| 4. |
Hegeman, A.D., Gross, J.W. and Frey, P.A. Probing catalysis by Escherichia coli dTDP-glucose-4,6-dehydratase: identification and preliminary characterization of functional amino acid residues at the active site. Biochemistry 40 (2001) 6598–6610. [DOI] [PMID: 11380254] |
| 5. |
Gross, J.W., Hegeman, A.D., Gerratana, B. and Frey, P.A. Dehydration is catalyzed by glutamate-136 and aspartic acid-135 active site residues in Escherichia coli dTDP-glucose 4,6-dehydratase. Biochemistry 40 (2001) 12497–12504. [DOI] [PMID: 11601973] |
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| [EC 4.2.1.46 created 1972] |
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