The Enzyme Database

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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
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, 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. [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. [PMID: 11601973]
[EC 4.2.1.46 created 1972]
 
 


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