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Literature summary extracted from

  • Thuy, T.T.; Liou, K.; Oh, T.J.; Kim, D.H.; Nam, D.H.; Yoo, J.C.; Sohng, J.K.
    Biosynthesis of dTDP-6-deoxy-beta-D-allose, biochemical characterization of dTDP-4-keto-6-deoxyglucose reductase (GerKI) from Streptomyces sp. KCTC 0041BP (2007), Glycobiology, 17, 119-126.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.364 expression in Escherichia coli BL21 Streptomyces sp.
5.1.3.27 expression in Escherichia coli BL21 Streptomyces sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.364 Mg2+
-
Streptomyces sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.364 52000
-
x * 52000, including the 6His-tag and thioredoxin-tagged fusion protein, SDS-PAGE Streptomyces sp.
5.1.3.27 38000
-
x * 38000, including the 6 His-tag and thioredoxin-tagged fusion protein, SDS-PAGE Streptomyces sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.364 dTDP-4-dehydro-6-deoxy-alpha-D-gulopyranose + NADH + H+ Streptomyces sp. the enzyme forms an activated deoxy-alpha-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II dTDP-6-deoxy-alpha-D-allopyranose + NAD+
-
?
5.1.3.27 dTDP-4-dehydro-6-deoxy-alpha-D-glucose Streptomyces sp. the enzyme is involved in the mycinose biosynthetic pathway of several macrolide antibiotics dTDP-4-dehydro-6-deoxy-beta-D-gulose
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.364 Streptomyces sp. Q331Q7
-
-
5.1.3.27 Streptomyces sp. Q331R1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.364 recombinant enzyme Streptomyces sp.
5.1.3.27 recombinant enzyme Streptomyces sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.364 dTDP-4-dehydro-6-deoxy-alpha-D-gulopyranose + NADH + H+ the enzyme forms an activated deoxy-alpha-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II Streptomyces sp. dTDP-6-deoxy-alpha-D-allopyranose + NAD+
-
?
1.1.1.364 dTDP-4-dehydro-6-deoxy-alpha-D-gulopyranose + NADH + H+ dTDP-4-dehydro-6-deoxy-alpha-D-gulose i.e. dTDP-4-dehydro-6-deoxy-alpha-D-allose Streptomyces sp. dTDP-6-deoxy-alpha-D-allopyranose + NAD+
-
?
5.1.3.27 dTDP-4-dehydro-6-deoxy-alpha-D-glucose the enzyme is involved in the mycinose biosynthetic pathway of several macrolide antibiotics Streptomyces sp. dTDP-4-dehydro-6-deoxy-beta-D-gulose
-
?
5.1.3.27 dTDP-4-dehydro-6-deoxy-alpha-D-glucose failures to acquire an isolation product from the GerF enzyme assay (detection of maltol, the decomposition product of the activated intermediate). However, the successful isolation of dTDP-6-deoxy-D-allose (in a coupled assay with GerKI) provides evidence sufficient to confirm that GerF functions as a dTDP-4-keto-6-deoxyglucose 3-epimerase in the mycinose biosynthesis pathway Streptomyces sp. dTDP-4-dehydro-6-deoxy-beta-D-gulose
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.364 ? x * 52000, including the 6His-tag and thioredoxin-tagged fusion protein, SDS-PAGE Streptomyces sp.
5.1.3.27 ? x * 38000, including the 6 His-tag and thioredoxin-tagged fusion protein, SDS-PAGE Streptomyces sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.1.364 GerKI
-
Streptomyces sp.
5.1.3.27 dTDP-4-keto-6-deoxyglucose 3-epimerase
-
Streptomyces sp.
5.1.3.27 GerF
-
Streptomyces sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.364 NADH
-
Streptomyces sp.

General Information

EC Number General Information Comment Organism
1.1.1.364 physiological function the enzyme forms an activated deoxy-alpha-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II Streptomyces sp.
5.1.3.27 physiological function the enzyme is involved in the mycinose biosynthetic pathway of several macrolide antibiotics Streptomyces sp.