EC |
1.1.1.384 |
Accepted name: |
dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose 3-reductase |
Reaction: |
dTDP-4-dehydro-2,6-dideoxy-α-D-glucose + NADP+ = dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose + NADPH + H+ |
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For diagram of dTDP-forosamine biosynthesis, click here |
Glossary: |
dTDP-4-dehydro-2,6-dideoxy-α-D-glucose = dTDP-2,6-dideoxy-α-D-threo-hexopyranos-4-ulose
dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose = thymidine 5′-[(2R,6R)-6-methyl-4,5-dioxotetrahydro-2H-pyran-2-yl] diphosphate
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Other name(s): |
KijD10; dTDP-4-keto-2,6-dideoxy-D-glucose 3-oxidoreductase; dTDP-4-dehydro-2,6-dideoxy-α-D-glucose 3-oxidoreductase |
Systematic name: |
dTDP-4-dehydro-2,6-dideoxy-α-D-glucose:NADP+ 3-oxidoreductase |
Comments: |
The enzyme is involved in the biosynthesis of several deoxysugars, including L-digitoxose, L- and D-olivose, L-oliose, D-mycarose and forosamine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Aguirrezabalaga, I., Olano, C., Allende, N., Rodriguez, L., Brana, A.F., Mendez, C. and Salas, J.A. Identification and expression of genes involved in biosynthesis of L-oleandrose and its intermediate L-olivose in the oleandomycin producer Streptomyces antibioticus. Antimicrob. Agents Chemother. 44 (2000) 1266–1275. [DOI] [PMID: 10770761] |
2. |
Wang, L., White, R.L. and Vining, L.C. Biosynthesis of the dideoxysugar component of jadomycin B: genes in the jad cluster of Streptomyces venezuelae ISP5230 for L-digitoxose assembly and transfer to the angucycline aglycone. Microbiology 148 (2002) 1091–1103. [DOI] [PMID: 11932454] |
3. |
Hong, L., Zhao, Z., Melancon, C.E., 3rd, Zhang, H. and Liu, H.W. In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa. J. Am. Chem. Soc. 130 (2008) 4954–4967. [DOI] [PMID: 18345667] |
4. |
Kubiak, R.L. and Holden, H.M. Combined structural and functional investigation of a C-3′′-ketoreductase involved in the biosynthesis of dTDP-L-digitoxose. Biochemistry 50 (2011) 5905–5917. [DOI] [PMID: 21598943] |
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[EC 1.1.1.384 created 2015] |
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EC |
4.2.1.164 |
Accepted name: |
dTDP-4-dehydro-2,6-dideoxy-D-glucose 3-dehydratase |
Reaction: |
dTDP-4-dehydro-2,6-dideoxy-α-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = dTDP-4-dehydro-2,3,6-trideoxy-α-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster |
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For diagram of dTDP-forosamine biosynthesis, click here |
Other name(s): |
SpnQ; TDP-4-keto-2,6-dideoxy-D-glucose 3-dehydrase |
Systematic name: |
dTDP-4-dehydro-2,6-dideoxy-α-D-glucose hydro-lyase (dTDP-2,3,6-trideoxy-α-D-hexopyranose-forming) |
Comments: |
A pyridoxal 5′-phosphate protein. The enzyme, isolated from the bacterium Saccharopolyspora spinosa, participates in the biosynthesis of forosamine. Requires ferredoxin/ferredoxin reductase or flavodoxin/flavodoxin reductase [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Hong, L., Zhao, Z. and Liu, H.W. Characterization of SpnQ from the spinosyn biosynthetic pathway of Saccharopolyspora spinosa: mechanistic and evolutionary implications for C-3 deoxygenation in deoxysugar biosynthesis. J. Am. Chem. Soc. 128 (2006) 14262–14263. [DOI] [PMID: 17076492] |
2. |
Hong, L., Zhao, Z., Melancon, C.E., 3rd, Zhang, H. and Liu, H.W. In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa. J. Am. Chem. Soc. 130 (2008) 4954–4967. [DOI] [PMID: 18345667] |
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[EC 4.2.1.164 created 2016] |
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