EC Number | Cloned (Comment) | Organism |
---|---|---|
5.3.2.3 | expression in Escherichia coli | Aneurinibacillus thermoaerophilus |
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 |
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 |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.3.2.3 | Aneurinibacillus thermoaerophilus | Q6T1W8 | - |
- |
5.3.2.3 | Aneurinibacillus thermoaerophilus L420-91T | Q6T1W8 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
5.3.2.3 | - |
Aneurinibacillus thermoaerophilus |
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 | - |
? |
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 |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.3.2.3 | 37 | - |
assay at | Aneurinibacillus thermoaerophilus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
5.3.2.3 | 7.5 | - |
assay at | Aneurinibacillus thermoaerophilus |