4.2.1.164: dTDP-4-dehydro-2,6-dideoxy-D-glucose 3-dehydratase
This is an abbreviated version!
For detailed information about dTDP-4-dehydro-2,6-dideoxy-D-glucose 3-dehydratase, go to the full flat file.
Reaction
+ 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = + + 2 oxidized ferredoxin [iron-sulfur] cluster
Synonyms
SpnQ
ECTree
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Substrates Products
Substrates Products on EC 4.2.1.164 - dTDP-4-dehydro-2,6-dideoxy-D-glucose 3-dehydratase
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REACTION DIAGRAM
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
additional information
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TDP-4-dehydro-6-deoxy-D-glucose is not a substrate
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dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
the enzyme participates in the biosynthesis of forosamine, a key structural component of the spinosyns, which are produced by Saccharopolyspora spinosa
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dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
the enzyme requires ferredoxin/ferredoxin reductase or flavodoxin/flavodoxin reductase. It can act as a transaminase when the electron-transfer path is blocked
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dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
the enzyme is involved in TDP-D-forosamine biosynthesis in the spinosyn pathway
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dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
the enzyme is capable of catalyzing C-3 deoxygenation in the presence of dithionite or the reductase pairs ferredoxin/ferredoxin reductase or flavodoxin/flavodoxin reductase. Conversion is significantly more efficient using reductase pairs than using dithionite. In the absence of an electron source and in the presence of L-glutamate, SpnQ catalyzes a transamination reaction, converting dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose to TDP-4-amino-2,4,6-trideoxy-D-glucose
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