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IUBMB 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 .
Reaction Schemes
+
2
reduced ferredoxin [iron-sulfur] cluster
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2
=
+
+
2
oxidized ferredoxin [iron-sulfur] cluster
Synonyms
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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
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MetaCyc
dTDP-alpha-D-forosamine biosynthesis
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dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose hydro-lyase (dTDP-2,3,6-trideoxy-alpha-D-hexopyranose-forming)
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].
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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
additional information
?
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Substrates: TDP-4-dehydro-6-deoxy-D-glucose is not a substrate
?
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
Substrates: the enzyme participates in the biosynthesis of forosamine, a key structural component of the spinosyns, which are produced by Saccharopolyspora spinosa
?
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
Substrates: the enzyme requires ferredoxin/ferredoxin reductase or flavodoxin/flavodoxin reductase. It can act as a transaminase when the electron-transfer path is blocked
?
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
Substrates: the enzyme is involved in TDP-D-forosamine biosynthesis in the spinosyn pathway
?
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
Substrates: 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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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
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
Substrates: the enzyme participates in the biosynthesis of forosamine, a key structural component of the spinosyns, which are produced by Saccharopolyspora spinosa
?
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
Substrates: the enzyme is involved in TDP-D-forosamine biosynthesis in the spinosyn pathway
?
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iron-sulfur centre
the enzyme contains 1.2 irons per monomer as determined by ferrozine quantitation, consistent with the enzyme having a [2Fe-2S] cluster
pyridoxal 5'-phosphate
a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
the enzyme is dependent on pyridoxal 5'-phosphate
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iron-sulfur centre
the enzyme contains 1.2 irons per monomer as determined by ferrozine quantitation, consistent with the enzyme having a [2Fe-2S] cluster
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additional information
the enzyme contains a [2Fe-2S] binding motif
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0.049
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose
pH 7.5, 24°C
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0.043
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose
pH 7.5, 24°C
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0.88
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose
pH 7.5, 24°C
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UniProt
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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metabolism
the enzyme participates in the biosynthesis of forosamine, a key structural component of the spinosyns, which are produced by Saccharopolyspora spinosa
metabolism
the enzyme is involved in TDP-D-forosamine biosynthesis in the spinosyn pathway
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SPNQ_SACSN
462
0
50385
Swiss-Prot
-
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51000
2 * 51000, SDS-PAGE
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dimer
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dimer
2 * 51000, SDS-PAGE
dimer
2 * 50361, calculated from sequence
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expressed in E. coli BL21(DE3) cells
expression in Escherichia coli BL21
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Hong, L.; Zhao, Z.; Melancon III, C.; Zhang, H.; Liu, H.
In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa
J. Am. Chem. Soc.
130
4954-4967
2008
Saccharopolyspora spinosa (Q9ALN8)
brenda
Hong L, H.L.; Zhao Z, Z.Z.; Liu H.-W, L.H.
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
14262-14263
2006
Saccharopolyspora spinosa (Q9ALN8)
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