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Literature summary extracted from

  • 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 (2006), J. Am. Chem. Soc., 128, 14262-14263.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.164 additional information the enzyme contains a [2Fe-2S] binding motif Saccharopolyspora spinosa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.164 expressed in E. coli BL21(DE3) cells Saccharopolyspora spinosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.164 dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Saccharopolyspora spinosa the enzyme participates in the biosynthesis of forosamine, a key structural component of the spinosyns, which are produced by Saccharopolyspora spinosa dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.159 Saccharopolyspora spinosa Q9ALN6
-
-
4.2.1.164 Saccharopolyspora spinosa Q9ALN8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.164
-
 Saccharopolyspora spinosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.159 dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose
-
 Saccharopolyspora spinosa dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H2O enzymes SpnO and SpnN are the 2,3-dehydratase and 3-ketoreductase, which together catalyze the conversion of dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose to 4-dehydro-2,6-dideoxy-D-glucose ?
4.2.1.164 dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ the enzyme participates in the biosynthesis of forosamine, a key structural component of the spinosyns, which are produced by Saccharopolyspora spinosa Saccharopolyspora spinosa dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
4.2.1.164 dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ the enzyme requires ferredoxin/ferredoxin reductase or flavodoxin/flavodoxin reductase. It can act as a transaminase when the electron-transfer path is blocked Saccharopolyspora spinosa dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.164 dimer
-
 Saccharopolyspora spinosa

Synonyms

EC Number Synonyms Comment Organism
4.2.1.159 spnO
-
 Saccharopolyspora spinosa
4.2.1.164 SpnQ
-
 Saccharopolyspora spinosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.164 25
-
 assay at Saccharopolyspora spinosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.164 7.5
-
 assay at Saccharopolyspora spinosa

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.164 pyridoxal 5'-phosphate a pyridoxal 5'-phosphate protein Saccharopolyspora spinosa

General Information

EC Number General Information Comment Organism
4.2.1.159 physiological function in forosamine biosynthesis, enzymes SpnO and SpnN function as a 2,3-dehydrase and a 3-ketoreductase, respectively. The two enzymes act sequentially to catalyze C-2 deoxygenation of TDP-4-dehydro-6-deoxy-D-glucose to form the SpnQ substrate, TDP-4-dehydro-2,6-dideoxy-D-glucose Saccharopolyspora spinosa
4.2.1.164 metabolism the enzyme participates in the biosynthesis of forosamine, a key structural component of the spinosyns, which are produced by Saccharopolyspora spinosa Saccharopolyspora spinosa