EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.20 | L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate | Escherichia coli | the tryptophan synthase alpha2beta2 bi-enzyme complex catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyzes cleavage of 3-indole-D-glycerol 3'-phosphate to give indole and D-glyceraldehyde 3'-phosphate. Indole is then transferred from the alpha-subunit to the beta-subunit where it reacts with L-Ser in a pyridoxal 5'-phosphate-dependent reaction to give L-Trp and a water molecule | L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
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EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.20 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.20 | L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate | the tryptophan synthase alpha2beta2 bi-enzyme complex catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyzes cleavage of 3-indole-D-glycerol 3'-phosphate to give indole and D-glyceraldehyde 3'-phosphate. Indole is then transferred from the alpha-subunit to the beta-subunit where it reacts with L-Ser in a pyridoxal 5'-phosphate-dependent reaction to give L-Trp and a water molecule | Escherichia coli | L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.2.1.20 | heterotetramer | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.20 | pyridoxal 5'-phosphate | dependent on | Escherichia coli |