The Enzyme Database

Your query returned 6 entries.    printer_iconPrintable version



EC 1.1.1.266     
Accepted name: dTDP-4-dehydro-6-deoxyglucose reductase
Reaction: dTDP-α-D-fucopyranose + NAD(P)+ = dTDP-4-dehydro-6-deoxy-α-D-glucose + NAD(P)H + H+
For diagram of dTDP-6-deoxyhexose biosynthesis, click here
Glossary: dTDP-4-dehydro-6-deoxy-α-D-glucose = dTDP-6-deoxy-α-D-xylo-hexopyranos-4-ulose = thymidine 5′-[3-(6-deoxy--D-xylo-hexopyranosyl-4-ulose) diphosphate]
Other name(s): dTDP-4-keto-6-deoxyglucose reductase; dTDP-D-fucose:NADP+ oxidoreductase; Fcf1; dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase
Systematic name: dTDP-α-D-fucopyranose:NAD(P)+ oxidoreductase
Comments: The enzymes from the Gram-negative bacteria Aggregatibacter actinomycetemcomitans and Escherichia coli O52 are involved in activation of fucose for incorporation into capsular polysaccharide O-antigens [1,3]. The enzyme from the Gram-positive bacterium Anoxybacillus tepidamans (Geobacillus tepidamans) is involved in activation of fucose for incorporation into the organism’s S-layer [2]. The enzyme from Escherichia coli O52 has a higher catalytic efficiency with NADH than with NADPH [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yoshida, Y., Nakano, Y., Nezu, T., Yamashita, Y. and Koga, T. A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose. J. Biol. Chem. 274 (1999) 16933–16939. [DOI] [PMID: 10358040]
2.  Zayni, S., Steiner, K., Pfostl, A., Hofinger, A., Kosma, P., Schaffer, C. and Messner, P. The dTDP-4-dehydro-6-deoxyglucose reductase encoding fcd gene is part of the surface layer glycoprotein glycosylation gene cluster of Geobacillus tepidamans GS5-97T. Glycobiology 17 (2007) 433–443. [DOI] [PMID: 17202151]
3.  Wang, Q., Ding, P., Perepelov, A.V., Xu, Y., Wang, Y., Knirel, Y.A., Wang, L. and Feng, L. Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52. Mol. Microbiol. 70 (2008) 1358–1367. [DOI] [PMID: 19019146]
[EC 1.1.1.266 created 2001, modified 2013]
 
 
EC 2.6.1.33     
Accepted name: dTDP-4-amino-4,6-dideoxy-D-glucose transaminase
Reaction: dTDP-4-amino-4,6-dideoxy-α-D-glucose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-α-D-glucose + L-glutamate
For diagram of dTDP-D-desosamine biosynthesis, click here
Other name(s): thymidine diphospho-4-amino-4,6-dideoxyglucose aminotransferase; thymidine diphospho-4-amino-6-deoxyglucose aminotransferase; thymidine diphospho-4-keto-6-deoxy-D-glucose transaminase; thymidine diphospho-4-keto-6-deoxy-D-glucose-glutamic transaminase; TDP-4-keto-6-deoxy-D-glucose transaminase; VioA; dTDP-4-amino-4,6-dideoxy-D-glucose:2-oxoglutarate aminotransferase
Systematic name: dTDP-4-amino-4,6-dideoxy-α-D-glucose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9023-19-2
References:
1.  Matsuhashi, M. and Strominger, J.L. Thymidine diphosphate 4-acetamido-2,6-dideoxyhexoses. 3. Purification and properties of thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase from Escherichia coli strain B. J. Biol. Chem. 241 (1966) 4738–4744. [PMID: 5332731]
2.  Wang, Y., Xu, Y., Perepelov, A.V., Qi, Y., Knirel, Y.A., Wang, L. and Feng, L. Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in Shigella dysenteriae type 7 and Escherichia coli O7. J. Bacteriol. 189 (2007) 8626–8635. [DOI] [PMID: 17905981]
[EC 2.6.1.33 created 1972]
 
 
EC 2.6.1.59     
Accepted name: dTDP-4-amino-4,6-dideoxygalactose transaminase
Reaction: dTDP-4-amino-4,6-dideoxy-α-D-galactose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-α-D-galactose + L-glutamate
For diagram of dTDP-Fuc3NAc, dTDP-Fuc4NAc and dTDP-Fuc3NMe2 biosynthesis, click here
Glossary: dTDP-4-dehydro-6-deoxy-α-D-galactose = dTDP-4-dehydro-6-deoxy-α-D-glucose
Other name(s): thymidine diphosphoaminodideoxygalactose aminotransferase; thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase; WecE; dTDP-4,6-dideoxy-D-galactose:2-oxoglutarate aminotransferase; dTDP-4,6-dideoxy-α-D-galactose:2-oxoglutarate aminotransferase
Systematic name: dTDP-4-amino-4,6-dideoxy-α-D-galactose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72560-97-5
References:
1.  Ohashi, H., Matsuhashi, M. and Matsuhashi, S. Thymidine diphosphate 4-acetamido-4,6-dideoxyhexoses. IV. Purification and properties of thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase from Pasteurella pseudotuberculosis. J. Biol. Chem. 246 (1971) 2325–2330. [PMID: 4928644]
2.  Hwang, B.Y., Lee, H.J., Yang, Y.H., Joo, H.S. and Kim, B.G. Characterization and investigation of substrate specificity of the sugar aminotransferase WecE from E. coli K12. Chem. Biol. 11 (2004) 915–925. [DOI] [PMID: 15271350]
[EC 2.6.1.59 created 1978]
 
 
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. [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]
[EC 4.2.1.46 created 1972]
 
 
EC 5.1.3.13     
Accepted name: dTDP-4-dehydrorhamnose 3,5-epimerase
Reaction: dTDP-4-dehydro-6-deoxy-α-D-glucose = dTDP-4-dehydro-β-L-rhamnose
For diagram of dtdp-6-deoxyhexose biosynthesis, click here and for diagram of 6-deoxyhexose biosynthesis, click here
Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
Other name(s): dTDP-L-rhamnose synthetase; dTDP-L-rhamnose synthase; thymidine diphospho-4-ketorhamnose 3,5-epimerase; TDP-4-ketorhamnose 3,5-epimerase; dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase; TDP-4-keto-L-rhamnose-3,5-epimerase
Systematic name: dTDP-4-dehydro-6-deoxy-α-D-glucose 3,5-epimerase
Comments: The enzyme occurs in a complex with EC 1.1.1.133 dTDP-4-dehydrorhamnose reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37318-39-1
References:
1.  Gaugler, R.W. and Gabriel, O. Biological mechanisms involved in the formation of deoxy sugars. VII. Biosynthesis of 6-deoxy-L-talose. J. Biol. Chem. 248 (1973) 6041–6049. [PMID: 4199258]
2.  Melo, A. and Glaser, L. The mechanism of 6-deoxyhexose synthesis. II. Conversion of deoxythymidine diphosphate 4-keto-6-deoxy-D-glucose to deoxythymidine diphosphate L-rhamnose. J. Biol. Chem. 243 (1968) 1475–1478. [PMID: 4384782]
[EC 5.1.3.13 created 1972]
 
 
EC 5.1.3.27     
Accepted name: dTDP-4-dehydro-6-deoxy-D-glucose 3-epimerase
Reaction: dTDP-4-dehydro-6-deoxy-α-D-glucose = dTDP-4-dehydro-6-deoxy-α-D-gulose
For diagram of dTDP-6-deoxy-α-D-allose biosynthesis, click here and for diagram of dTDP-6-deoxyhexose biosynthesis, click here
Glossary: dTDP-4-dehydro-6-deoxy-α-D-gulose = dTDP-4-dehydro-6-deoxy-α-D-allose
Other name(s): dTDP-deoxyglucose 3-epimerase; dTDP-4-keto-6-deoxy-D-glucose 3-epimerase; dTDP-4-keto-6-deoxyglucose 3-epimerase; gerF (gene name); tylJ (gene name); chmJ (gene name); mydH (gene name)
Systematic name: dTDP-4-dehydro-6-deoxy-α-D-glucose 3-epimerase
Comments: The enzyme is involved in the biosynthetic pathway of dTDP-6-deoxy-α-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sohng, J.K., Kim, H.J., Nam, D.H., Lim, D.O., Han, J.M., Lee, H.J. and Yoo, J.C. Cloning, expression, and biological function of a dTDP-deoxyglucose epimerase (gerF) gene from Streptomyces sp. GERI-155. Biotechnol. Lett. 26 (2004) 185–191. [PMID: 15049360]
2.  Thuy, T.T., Liou, K., Oh, T.J., Kim, D.H., Nam, D.H., Yoo, J.C. and Sohng, J.K. Biosynthesis of dTDP-6-deoxy-β-D-allose, biochemical characterization of dTDP-4-keto-6-deoxyglucose reductase (GerKI) from Streptomyces sp. KCTC 0041BP. Glycobiology 17 (2007) 119–126. [DOI] [PMID: 17053005]
3.  Kubiak, R.L., Phillips, R.K., Zmudka, M.W., Ahn, M.R., Maka, E.M., Pyeatt, G.L., Roggensack, S.J. and Holden, H.M. Structural and functional studies on a 3′-epimerase involved in the biosynthesis of dTDP-6-deoxy-D-allose. Biochemistry 51 (2012) 9375–9383. [DOI] [PMID: 23116432]
[EC 5.1.3.27 created 2013]
 
 


Data © 2001–2021 IUBMB
Web site © 2005–2021 Andrew McDonald