EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.7.1.50 | crystallization by vapor diffusion equilibration, crystal structure at 1.5 A resolution | Bacillus subtilis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.50 | ATP + 4-methyl-5-(2-hydroxyethyl)thiazole | Bacillus subtilis | the enzyme is a salvage enzyme in the thiamin biosynthetic pathway and enables the cell to use recycled 4-methyl-5-beta-hydroxyethylthiazole as an alternative to its synthesis from 1-deoxy-D-xylulose-5-phosphate, cysteine, and tyrosine | ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.1.50 | Bacillus subtilis | P39593 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.50 | ATP + 4-methyl-5-(2-hydroxyethyl)thiazole | phosphate transfer occurs by an inline mechanism | Bacillus subtilis | ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole | - |
? | |
2.7.1.50 | ATP + 4-methyl-5-(2-hydroxyethyl)thiazole | the enzyme is a salvage enzyme in the thiamin biosynthetic pathway and enables the cell to use recycled 4-methyl-5-beta-hydroxyethylthiazole as an alternative to its synthesis from 1-deoxy-D-xylulose-5-phosphate, cysteine, and tyrosine | Bacillus subtilis | ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.1.50 | More | as determined from crystallization data the enzyme is a trimer of identical subunits, the active site is formed at the interface between two subunits within the trimer | Bacillus subtilis |