| Tryptophan synthase (indole-salvaging) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.1.122 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Tryptophan synthase (indole-salvaging) ( EC 4.2.1.122, tryptophan synthase beta2) is an enzyme with systematic name L-serine hydro-lyase (adding indole, L-tryptophan-forming). [1] This enzyme catalyses the following chemical reaction
- L- serine + indole L- tryptophan + H2O
This enzyme salvages the lost indole to L-tryptophan.
References
- ^ Hettwer S, Sterner R (March 2002). "A novel tryptophan synthase β-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role". The Journal of Biological Chemistry. 277 (10): 8194–201. doi: 10.1074/jbc.m111541200. PMID 11756459.
External links
- Tryptophan+synthase+(indole-salvaging) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Tryptophan synthase (indole-salvaging) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.1.122 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Tryptophan synthase (indole-salvaging) ( EC 4.2.1.122, tryptophan synthase beta2) is an enzyme with systematic name L-serine hydro-lyase (adding indole, L-tryptophan-forming). [1] This enzyme catalyses the following chemical reaction
- L- serine + indole L- tryptophan + H2O
This enzyme salvages the lost indole to L-tryptophan.
References
- ^ Hettwer S, Sterner R (March 2002). "A novel tryptophan synthase β-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role". The Journal of Biological Chemistry. 277 (10): 8194–201. doi: 10.1074/jbc.m111541200. PMID 11756459.
External links
- Tryptophan+synthase+(indole-salvaging) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)