EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.2.8 | expressed in Escherichia coli | Zea mays |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.1.2.8 | the crystal structure of BX1 suggusts that the faster catalytic rate of BX1 compared to the homologous alpha-subuni8t of tryptophan synthase EC 4.2.1.20, may due to a stabilzation of the active conformation, loop alphaL6 is closed and the catalytic glutamate, Glu134 is in the active conformation. There are two crystallographically independent molecules in the asymmetric unit of the rhombohedral BX1 crystal form | Zea mays |
4.2.1.20 | crystal structures of the alpha-subunit of tryptophan synthase alone and in the alpha2beta2 complex | Salmonella enterica subsp. enterica serovar Typhimurium |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
4.1.2.8 | plastid | - |
Zea mays | 9536 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.2.8 | indole-3-glycerol phosphate | Zea mays | the indole is further converted to 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, a secondary plant metabolite. BX1 cleaves indole-3-glycerol phosphate significantly faster to indole and glyceraldehyde 3-phosphate than the homologous alpha-subunit of tryptophan synthase, EC 4.2.1.20 | indole + glyceraldehyde 3-phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.2.8 | Zea mays | P42390 | - |
- |
4.2.1.20 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.2.8 | - |
Zea mays |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.1.2.8 | (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate | the indole is further converted to 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, a secondary plant metabolite. BX1 cleaves indole-3-glycerol phosphate significantly faster to indole and glyceraldehyde 3-phosphate than the homologous alpha-subunit of tryptophan synthase, EC 4.2.1.20. In the primary metabolism, indole diffuses through the connecting tunnel to the beta-active site where it is condensed with serine to form tryptophan and water | Zea mays |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.1.2.8 | seedling | - |
Zea mays | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.2.8 | indole-3-glycerol phosphate | - |
Zea mays | indole + glyceraldehyde 3-phosphate | - |
? | |
4.1.2.8 | indole-3-glycerol phosphate | the indole is further converted to 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, a secondary plant metabolite. BX1 cleaves indole-3-glycerol phosphate significantly faster to indole and glyceraldehyde 3-phosphate than the homologous alpha-subunit of tryptophan synthase, EC 4.2.1.20 | Zea mays | indole + glyceraldehyde 3-phosphate | - |
? | |
4.2.1.20 | indole-3-glycerol phosphate | reaction is catalyzed by alpha-subunit. Structural basis of the catalytic mechanism and regulation of the alpha-subunit | Salmonella enterica subsp. enterica serovar Typhimurium | indole + D-glyceraldehyde 3-phosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.2.8 | BX1 | a homolog of the alpha-subunit of bifunctional trypthophan synthase | Zea mays |
4.2.1.20 | TRPS | - |
Salmonella enterica subsp. enterica serovar Typhimurium |