Protein Variants | Comment | Organism |
---|---|---|
D305A | mutation of a beta-subunit residue, no active site residue, altered subunit interaction | Escherichia coli |
E109D | mutation of a beta-subunit active site residue, reduced reach and conformational freedom of the carboxylate functionality, accumulation of indole at the beta-site | Escherichia coli |
K87T | mutation of a beta-subunit active site residue, inactive mutant, which can form an external aldimine, but cannot form an alpha-aminoacrylate intermediate | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8) | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-(indol-3-yl)glycerol 3-phosphate | alpha-subunit of the bienzyme complex, alpha-reaction | Escherichia coli | D-glyceraldehyde 3-phosphate + indole | - |
? | |
L-serine + indole | beta-subunit of the bienzyme complex, beta-reaction | Escherichia coli | L-tryptophan + H2O | - |
? | |
additional information | enzyme switches between open inactive conformation and closed active conformation, overview | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | NMR measurement and determination of wild-type and mutant enzyme structures, complexed with L-tryptophane, in presence or absence of allosteric ligands, such as Na+, NH4+, Cs+, and DL_alpha-glycerol 3-phosphate, overview | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Escherichia coli |