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Literature summary extracted from
- X-ray structures of Bacillus pallidus D-arabinose isomerase and its complex with L-fucitol (2010), Biochim. Biophys. Acta, 1804, 1359-1368.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.3.1.3 | for over-expression in Escherichia coli JM109 cells | Aeribacillus pallidus |
| 5.3.1.25 | for over-expression in Escherichia coli JM109 cells | Aeribacillus pallidus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.3.1.3 | three X-ray structures of D-arabinose isomerase in complexes with 2-methyl-2,4-pentadiol, glycerol and L-fucitol are determined at resolutions of 1.77, 1.60 and 2.60 A, respectively | Aeribacillus pallidus |
| 5.3.1.25 | three X-ray structures of D-arabinose isomerase in complexes with 2-methyl-2,4-pentadiol, glycerol and L-fucitol are determined at resolutions of 1.77, 1.60 and 2.60 A, respectively | Aeribacillus pallidus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.1.3 | L-fucitol | - |
Aeribacillus pallidus |  |
| 5.3.1.25 | L-fucitol | - |
Aeribacillus pallidus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.1.3 | Mn2+ | - |
Aeribacillus pallidus | |
| 5.3.1.25 | Mn2+ | - |
Aeribacillus pallidus | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.3 | D-altrose | Aeribacillus pallidus | - |
D-psicose | - |
? | |
| 5.3.1.3 | D-arabinose | Aeribacillus pallidus | - |
D-ribulose | - |
? | |
| 5.3.1.25 | L-Fucose | Aeribacillus pallidus | - |
L-Fuculose | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.1.3 | Aeribacillus pallidus | C0SSE7 | - |
- |
| 5.3.1.25 | Aeribacillus pallidus | C0SSE7 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.3.1.3 | using an anion-exchange column, Q Sepharose high performance, a hydrophobic interaction column, RESOURCE PHE, and an anion-exchange column, RESOURCE Q | Aeribacillus pallidus |
| 5.3.1.25 | using an anion-exchange column, Q Sepharose high performance, a hydrophobic interaction column, RESOURCE PHE, and an anion-exchange column, RESOURCE Q | Aeribacillus pallidus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.3 | D-altrose | - |
Aeribacillus pallidus | D-psicose | - |
? | |
| 5.3.1.3 | D-arabinose | - |
Aeribacillus pallidus | D-ribulose | - |
? | |
| 5.3.1.25 | L-Fucose | - |
Aeribacillus pallidus | L-Fuculose | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.3.1.3 | homohexamer | - |
Aeribacillus pallidus |
| 5.3.1.25 | homohexamer | - |
Aeribacillus pallidus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.1.3 | D-Arabinose isomerase | L-fucose isomerase, bifunctional enzyme | Aeribacillus pallidus |
| 5.3.1.25 | L-Fucose isomerase | D-arabinose isomerase, bifunctional enzyme | Aeribacillus pallidus |
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Release 2023.1 (January 2023)
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