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Literature summary for 4.2.1.164 extracted from

  • 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 (2008), J. Am. Chem. Soc., 130, 4954-4967.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 Saccharopolyspora spinosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.049
-
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose pH 7.5, 24°C Saccharopolyspora spinosa

Metals/Ions

Metals/Ions Comment Organism Structure
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 Saccharopolyspora spinosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51000
-
2 * 51000, SDS-PAGE Saccharopolyspora spinosa
109400
-
-
Saccharopolyspora spinosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Saccharopolyspora spinosa the enzyme is involved in TDP-D-forosamine biosynthesis in the spinosyn pathway dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?

Organism

Organism UniProt Comment Textmining
Saccharopolyspora spinosa Q9ALN8
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharopolyspora spinosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ the enzyme is involved in TDP-D-forosamine biosynthesis in the spinosyn pathway Saccharopolyspora spinosa 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+ 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 Saccharopolyspora spinosa dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
additional information TDP-4-dehydro-6-deoxy-D-glucose is not a substrate Saccharopolyspora spinosa ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 51000, SDS-PAGE Saccharopolyspora spinosa
dimer 2 * 50361, calculated from sequence Saccharopolyspora spinosa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.043
-
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose pH 7.5, 24°C Saccharopolyspora spinosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Saccharopolyspora spinosa

Cofactor

Cofactor Comment Organism Structure
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 Saccharopolyspora spinosa
pyridoxal 5'-phosphate the enzyme is dependent on pyridoxal 5'-phosphate Saccharopolyspora spinosa

General Information

General Information Comment Organism
metabolism the enzyme is involved in TDP-D-forosamine biosynthesis in the spinosyn pathway Saccharopolyspora spinosa

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.88
-
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose pH 7.5, 24°C Saccharopolyspora spinosa