EC |
1.1.1.120 |
Accepted name: |
galactose 1-dehydrogenase (NADP+) |
Reaction: |
D-galactose + NADP+ = D-galactono-1,5-lactone + NADPH + H+ |
Other name(s): |
D-galactose dehydrogenase (NADP+); galactose 1-dehydrogenase (NADP) |
Systematic name: |
D-galactose:NADP+ 1-oxidoreductase |
Comments: |
Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-51-4 |
References: |
1. |
Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488–4492. [PMID: 5845847] |
2. |
Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493–4497. [PMID: 5845848] |
3. |
Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498–4502. [PMID: 5845849] |
4. |
Schiwara, H.W. and Domagk, G.F. Über den Abbau der Desoxyzucker durch Bakterienenzyme. V. Anreicherung und Charakterisierung einer NADP-abhängigen Abequosedehydrogenase aus Pseudomonas putida. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1321–1329. [PMID: 4387016] |
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[EC 1.1.1.120 created 1972] |
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EC |
1.1.1.341 |
Accepted name: |
CDP-abequose synthase |
Reaction: |
CDP-α-D-abequose + NADP+ = CDP-4-dehydro-3,6-dideoxy-α-D-glucose + NADPH + H+ |
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For diagram of CDP-abequose, CDP-ascarylose, CDP-paratose and CDP-tyrelose biosynthesis, click here |
Glossary: |
CDP-α-D-abequose = CDP-3,6-dideoxy-α-D-xylo-hexose |
Other name(s): |
rfbJ (gene name) |
Systematic name: |
CDP-α-D-abequose:NADP+ 4-oxidoreductase |
Comments: |
Isolated from Yersinia pseudotuberculosis [1,3] and Salmonella enterica [1,2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kessler, A.C., Brown, P.K., Romana, L.K. and Reeves, P.R. Molecular cloning and genetic characterization of the rfb region from Yersinia pseudotuberculosis serogroup IIA, which determines the formation of the 3,6-dideoxyhexose abequose. J. Gen. Microbiol. 137 (1991) 2689–2695. [DOI] [PMID: 1724263] |
2. |
Wyk, P. and Reeves, P. Identification and sequence of the gene for abequose synthase, which confers antigenic specificity on group B salmonellae: homology with galactose epimerase. J. Bacteriol. 171 (1989) 5687–5693. [DOI] [PMID: 2793832] |
3. |
Thorson, J.S., Lo, S.F., Ploux, O., He, X. and Liu, H.W. Studies of the biosynthesis of 3,6-dideoxyhexoses: molecular cloning and characterization of the asc (ascarylose) region from Yersinia pseudotuberculosis serogroup VA. J. Bacteriol. 176 (1994) 5483–5493. [DOI] [PMID: 8071227] |
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[EC 1.1.1.341 created 2012] |
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EC |
1.1.1.342 |
Accepted name: |
CDP-paratose synthase |
Reaction: |
CDP-α-D-paratose + NADP+ = CDP-4-dehydro-3,6-dideoxy-α-D-glucose + NADPH + H+ |
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For diagram of CDP-abequose, CDP-ascarylose, CDP-paratose and CDP-tyrelose biosynthesis, click here |
Glossary: |
CDP-α-D-paratose = CDP-3,6-dideoxy-α-D-glucose = CDP-3,6-dideoxy-α-D-ribo-hexose |
Other name(s): |
rfbS (gene name) |
Systematic name: |
CDP-α-D-paratose:NADP+ 4-oxidoreductase |
Comments: |
The enzyme is involved in synthesis of paratose and tyvelose, unusual 3,6-dideoxyhexose sugars that form part of the O-antigen in the lipopolysaccharides of several enteric bacteria. Isolated from Salmonella enterica subsp. enterica serovar Typhi (Salmonella typhi). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Verma, N. and Reeves, P. Identification and sequence of rfbS and rfbE, which determine antigenic specificity of group A and group D salmonellae. J. Bacteriol. 171 (1989) 5694–5701. [DOI] [PMID: 2793833] |
2. |
Hallis, T.M., Lei, Y., Que, N.L. and Liu, H. Mechanistic studies of the biosynthesis of paratose: purification and characterization of CDP-paratose synthase. Biochemistry 37 (1998) 4935–4945. [DOI] [PMID: 9538012] |
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[EC 1.1.1.342 created 2012] |
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EC |
1.17.1.1 |
Accepted name: |
CDP-4-dehydro-6-deoxyglucose reductase |
Reaction: |
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+ |
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For diagram of the biosynthesis of CDP-abequose, CDP-ascarylose, CDP-paratose and CDP-tyvelose, click here |
Other name(s): |
CDP-4-keto-6-deoxyglucose reductase; cytidine diphospho-4-keto-6-deoxy-D-glucose reductase; cytidine diphosphate 4-keto-6-deoxy-D-glucose-3-dehydrogenase; CDP-4-keto-deoxy-glucose reductase; CDP-4-keto-6-deoxy-D-glucose-3-dehydrogenase system; NAD(P)H:CDP-4-keto-6-deoxy-D-glucose oxidoreductase |
Systematic name: |
CDP-4-dehydro-3,6-dideoxy-D-glucose:NAD(P)+ 3-oxidoreductase |
Comments: |
The enzyme consists of two proteins. One forms an enzyme-bound adduct of the CDP-4-dehydro-6-deoxyglucose with pyridoxamine phosphate, in which the 3-hydroxy group has been removed. The second catalyses the reduction of this adduct by NAD(P)H and release of the CDP-4-dehydro-3,6-dideoxy-D-glucose and pyridoxamine phosphate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-87-4 |
References: |
1. |
Pape, H. and Strominger, J.L. Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. V. Partial purification of the two protein components required for introduction of the 3-deoxy group. J. Biol. Chem. 244 (1969) 3598–3604. [PMID: 4389672] |
2. |
Rubenstein, P.A. and Strominger, J.L. Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. VII. Mechanistic roles of enzyme E1 and pyridoxamine 5′-phosphate in the formation of cytidine diphosphate-4-keto-3,6-dideoxy-D-glucose from cytidine diphosphate-4-keto-6-deoxy-D-glucose. J. Biol. Chem. 249 (1974) 3776–3781. [PMID: 4152100] |
3. |
Liu, H.-W. and Thorson, J.S. Pathways and mechanisms in the biogenesis of novel deoxysugars by bacteria. Annu. Rev. Microbiol. 48 (1994) 223–256. [DOI] [PMID: 7826006] |
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[EC 1.17.1.1 created 1972, modified 2005] |
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EC |
2.4.1.60 |
Accepted name: |
CDP-abequose:α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase |
Reaction: |
CDP-α-D-abequose + α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = CDP + α-D-Abe-(1→3)-α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und |
Glossary: |
D-abequose = 3,6-deoxy-D-xylo-hexose = 3,6-deoxy-D-galactose = 3-deoxy-D-fucose
α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
α-D-Abe-(1→3)-α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-D-abequopyranosyl-(1→3)-α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol |
Other name(s): |
wbaV (gene name); rfbV (gene name); trihexose diphospholipid abequosyltransferase; abequosyltransferase (ambiguous); CDP-α-D-abequose:Man(α1→4)Rha(α1→3)Gal(β-1)-diphospholipid D-abequosyltransferase |
Systematic name: |
CDP-α-D-abequose:α-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 3III-α-abequosyltransferase (configuration retaining) |
Comments: |
The enzyme from Salmonella participates in the biosynthesis of the repeat unit of O antigens produced by strains that belong to the A, B and D1-D3 groups. The enzyme is able to transfer abequose, paratose, or tyvelose, depending on the availability of the specific dideoxyhexose in a particular strain. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-67-1 |
References: |
1. |
Osborn, M.J. and Weiner, I.M. Biosynthesis of a bacterial lipopolysaccharide. VI. Mechanism of incorporation of abequose into the O-antigen of Salmonella typhimurium. J. Biol. Chem. 243 (1968) 2631–2639. [PMID: 4297268] |
2. |
Liu, D., Lindqvist, L. and Reeves, P.R. Transferases of O-antigen biosynthesis in Salmonella enterica: dideoxyhexosyltransferases of groups B and C2 and acetyltransferase of group C2. J. Bacteriol. 177 (1995) 4084–4088. [DOI] [PMID: 7541787] |
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[EC 2.4.1.60 created 1972, modified 2012, modified 2021] |
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EC |
2.4.1.382 |
Accepted name: |
CDP-abequose:α-L-Rha2OAc-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase |
Reaction: |
CDP-α-D-abequose + 2-O-acetyl-α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = CDP + α-D-Abe-(1→3)-2-O-acetyl-α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und |
Glossary: |
α-L-Rha2OAc-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = 2-O-acetyl-α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
α-D-Abe-(1→3)-2-O-acetyl-α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und = α-D-abequosyl-(1→3)-2-O-acetyl-α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol |
Other name(s): |
wbaR (gene name); rfbR (gene name) |
Systematic name: |
CDP-α-D-abequose:2-O-acetyl-α-L-rhamnopyranosyl-(1→2)-α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 3IV-α-abequosyltransferase (configuration retaining) |
Comments: |
The enzyme, present in Salmonella strains that belong to group C2, participates in the biosynthesis of the repeat unit of O antigens produced by these strains. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Liu, D., Lindqvist, L. and Reeves, P.R. Transferases of O-antigen biosynthesis in Salmonella enterica: dideoxyhexosyltransferases of groups B and C2 and acetyltransferase of group C2. J. Bacteriol. 177 (1995) 4084–4088. [DOI] [PMID: 7541787] |
2. |
Zhao, X., Dai, Q., Jia, R., Zhu, D., Liu, M., Wang, M., Chen, S., Sun, K., Yang, Q., Wu, Y. and Cheng, A. two novel Salmonella bivalent vaccines confer dual protection against two Salmonella serovars in mice. Front Cell Infect Microbiol 7:391 (2017). [DOI] [PMID: 28929089] |
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[EC 2.4.1.382 created 2021] |
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EC |
2.7.7.33 |
Accepted name: |
glucose-1-phosphate cytidylyltransferase |
Reaction: |
CTP + α-D-glucose 1-phosphate = diphosphate + CDP-glucose |
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For diagram of CDP-abequose, CDP-ascarylose, CDP-paratose and CDP-tyrelose biosynthesis, click here |
Other name(s): |
CDP glucose pyrophosphorylase; cytidine diphosphoglucose pyrophosphorylase; cytidine diphosphate glucose pyrophosphorylase; cytidine diphosphate-D-glucose pyrophosphorylase; CTP:D-glucose-1-phosphate cytidylyltransferase |
Systematic name: |
CTP:α-D-glucose-1-phosphate cytidylyltransferase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-10-5 |
References: |
1. |
Mayer, R.M. and Ginsburg, V. Purification and properties of cytidine diphosphate D-glucose pyrophosphorylase from Salmonella paratyphi A. J. Biol. Chem. 240 (1965) 1900–1904. [PMID: 14299608] |
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[EC 2.7.7.33 created 1972] |
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EC |
4.2.1.45 |
Accepted name: |
CDP-glucose 4,6-dehydratase |
Reaction: |
CDP-glucose = CDP-4-dehydro-6-deoxy-D-glucose + H2O |
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For diagram of CDP-abequose, CDP-ascarylose, CDP-paratose and CDP-tyrelose biosynthesis, click here |
Other name(s): |
cytidine diphosphoglucose oxidoreductase; CDP-glucose 4,6-hydro-lyase |
Systematic name: |
CDP-glucose 4,6-hydro-lyase (CDP-4-dehydro-6-deoxy-D-glucose-forming) |
Comments: |
Requires bound NAD+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37259-55-5 |
References: |
1. |
Hey, A.E. and Elbein, A.D. Biosynthesis of tyvelose. The purification and properties of cytidine diphosphate D-glucose oxidoreductase. J. Biol. Chem. 241 (1966) 5473–5478. [PMID: 4380946] |
2. |
Matsuhashi, S., Matsuhashi, M., Brown, J.G. and Strominger, J.L. Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. 3. Cytidine diphosphate D-glucose oxidoreductase. J. Biol. Chem. 241 (1966) 4283–4287. [PMID: 4288651] |
3. |
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] |
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[EC 4.2.1.45 created 1972] |
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EC |
5.1.3.10 |
Accepted name: |
CDP-paratose 2-epimerase |
Reaction: |
CDP-α-D-paratose = CDP-α-D-tyvelose |
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For diagram of CDP-abequose, CDP-ascarylose, CDP-paratose and CDP-tyrelose biosynthesis, click here |
Glossary: |
CDP-α-D-tyvelose = CDP-3,6-dideoxy-α-D-mannose = CDP-3,6-dideoxy-α-D-arabino-hexose
CDP-α-D-paratose = CDP-3,6-dideoxy-α-D-glucose = CDP-3,6-dideoxy-α-D-ribo-hexose |
Other name(s): |
CDP-paratose epimerase; cytidine diphosphoabequose epimerase; cytidine diphosphodideoxyglucose epimerase; cytidine diphosphoparatose epimerase; cytidine diphosphate paratose-2-epimerase; CDP-abequose epimerase (incorrect); CDP-D-abequose 2-epimerase (incorrect); CDP-tyvelose 2-epimerase, |
Systematic name: |
CDP-3,6-dideoxy-D-glucose 2-epimerase |
Comments: |
Requires NAD+. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37318-36-8 |
References: |
1. |
Matsuhashi, S. Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. II. Reversible 2-epimerization of cytidine diphosphate paratose. J. Biol. Chem. 241 (1966) 4275–4282. [PMID: 5924649] |
2. |
Liu, H.-W. and Thorson, J.S. Pathways and mechanisms in the biogenesis of novel deoxysugars by bacteria. Annu. Rev. Microbiol. 48 (1994) 223–256. [DOI] [PMID: 7826006] |
3. |
Koropatkin, N.M., Liu, H.W. and Holden, H.M. High resolution x-ray structure of tyvelose epimerase from Salmonella typhi. J. Biol. Chem. 278 (2003) 20874–20881. [DOI] [PMID: 12642575] |
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[EC 5.1.3.10 created 1972, modified 2005] |
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