The Enzyme Database

Your query returned 2 entries.    printer_iconPrintable version

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+
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
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]
[EC 1.1.1.384 created 2015]
 
 
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
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]
[EC 4.2.1.164 created 2016]
 
 


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