Protein Variants | Comment | Organism |
---|---|---|
Y72F | site-directed mutagenesis, the replacement leads to a drastic decrease in activity for L-tryptophan by 50000fold. On the other hand considerable activities are retained with respect to substrates bearing good leaving groups and to L-serine. Kinetics show a coexistence of induced fit and selected fit in the reaction mechanism of a mutant tryptophan indole lyase Y72F, analysis of interaction of the mutant tryptophan indole-lyase (TIL) from Proteus vulgaris Y72F with the transition state analogue, oxindolyl-L-alanine (OIA), with the natural substrate, L-tryptophan, and with a substrate S-ethyl-L-cysteine, overview. The change of Tyr 72 to Phe leads to a considerable increase in the enzyme affinity to OIA, and to a very strong decrease of kf and kr values | Proteus vulgaris |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
oxindolyl-L-alanine | OIA, a transition state analogue, serves as substrate and inhibitor for enzyme mutant Y72F and wild-type enzyme | Proteus vulgaris |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | binding kinetics of enzyme mutant Y72F with substrates L-tryptophan, S-ethyl-L-cysteine, and oxindolyl-L-alanine, overview | Proteus vulgaris |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-tryptophan + H2O | Proteus vulgaris | - |
indole + pyruvate + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Proteus vulgaris | P28796 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-tryptophan + H2O | - |
Proteus vulgaris | indole + pyruvate + NH3 | - |
? | |
additional information | the enzyme is capable to catalyze alpha,beta-elimination reactions with a number of other amino acids, containing better leaving groups compared to L-tryptophan, e.g. S-ethyl-L-cysteine. For the wild-type enzyme the reactions with substrates are described by the same kinetic scheme where binding of holoenzyme with an amino acid, leading to reversible formation of an external aldimine, proceeds very fast, while following transformations, leading finally to reversible formation of a quinonoid intermediate proceed with measureable rates | Proteus vulgaris | ? | - |
? | |
oxindolyl-L-alanine + H2O | OIA, transition state analogue, the reaction of enzyme TIL mutant Y72F with OIA is accompanied by the appearance of intense absorption at 509 nm which may be explained by the formation of a quinonoid intermediate, transformation of the external aldimine into the quinonoid intermediate implies the transfer of alpha-proton to the base-acceptor in the active site. Oxindolyl-L-alanine also inhibits the enzyme | Proteus vulgaris | ? | - |
? | |
S-ethyl-L-cysteine + H2O | S-ethyl-L-cysteine represents a substrate with a better leaving group as compared to L-tryptophan | Proteus vulgaris | ethanethiol + pyruvate + NH3 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
TIL | - |
Proteus vulgaris |
tryptophan indole lyase | - |
Proteus vulgaris |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Proteus vulgaris |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
assay at | Proteus vulgaris |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | dependent on | Proteus vulgaris |