| 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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