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Literature summary extracted from

  • Davis, M.L.; Thoden, J.B.; Holden, H.M.
    The X-ray structure of dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase (2007), J. Biol. Chem., 282, 19227-19236.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.2.3 expression in Escherichia coli Aneurinibacillus thermoaerophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.2.3 crystallization of wild-type and selenomethionine-labeled FdtA, crystallization of the mutant proteins (H49N, H51N, H49N/H51N), hanging-drop method of vapor diffusion, crystallization trials are conducted at both 25°C and 4°C. Three-dimensional structure of this sugar isomerase complexed with dTDP and solved to 1.5 A resolution. Crystals belong to the space group P4(1)2(1)2 with unit cell dimensions of a = b = 62.7 A and c = 201.3 A and one dimer per asymmetric unit Aneurinibacillus thermoaerophilus

Protein Variants

EC Number Protein Variants Comment Organism
5.3.2.3 H49N complete loss of activity Aneurinibacillus thermoaerophilus
5.3.2.3 H49N/H51N complete loss of activity Aneurinibacillus thermoaerophilus
5.3.2.3 H51N mutant retains some activity Aneurinibacillus thermoaerophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.2.3 dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose Aneurinibacillus thermoaerophilus the enzyme is involved in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose. Four moieties of alpha-D-rhamnose and two moities of 3-acetamido-3,6-dideoxy-alpha-D-galactose form the repeating unit of the glycan chain in the S-layer of the bacterium Aneurinibacillus thermoaerophilus dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose
-
?
5.3.2.3 dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose Aneurinibacillus thermoaerophilus L420-91T the enzyme is involved in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose. Four moieties of alpha-D-rhamnose and two moities of 3-acetamido-3,6-dideoxy-alpha-D-galactose form the repeating unit of the glycan chain in the S-layer of the bacterium Aneurinibacillus thermoaerophilus dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose
-
?

Organism

EC Number Organism UniProt Comment Textmining
5.3.2.3 Aneurinibacillus thermoaerophilus Q6T1W8
-
-
5.3.2.3 Aneurinibacillus thermoaerophilus L420-91T Q6T1W8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.2.3
-
Aneurinibacillus thermoaerophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.2.3 dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose the enzyme is involved in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose. Four moieties of alpha-D-rhamnose and two moities of 3-acetamido-3,6-dideoxy-alpha-D-galactose form the repeating unit of the glycan chain in the S-layer of the bacterium Aneurinibacillus thermoaerophilus Aneurinibacillus thermoaerophilus dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose
-
?
5.3.2.3 dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose Site-directed mutagenesis experiments, enzymatic assays, and X-ray crystallographic analyses suggest that His49 functions as an active site base Aneurinibacillus thermoaerophilus dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose
-
?
5.3.2.3 dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose the enzyme is involved in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose. Four moieties of alpha-D-rhamnose and two moities of 3-acetamido-3,6-dideoxy-alpha-D-galactose form the repeating unit of the glycan chain in the S-layer of the bacterium Aneurinibacillus thermoaerophilus Aneurinibacillus thermoaerophilus L420-91T dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose
-
?
5.3.2.3 dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose Site-directed mutagenesis experiments, enzymatic assays, and X-ray crystallographic analyses suggest that His49 functions as an active site base Aneurinibacillus thermoaerophilus L420-91T dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose
-
?

Subunits

EC Number Subunits Comment Organism
5.3.2.3 dimer formation of the FdtA dimer represents a classical example of domain swapping whereby beta-strands 2 and 3 from one subunit form part of a beta-sheet in the second subunit Aneurinibacillus thermoaerophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.3.2.3 37
-
assay at Aneurinibacillus thermoaerophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.2.3 7.5
-
assay at Aneurinibacillus thermoaerophilus