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Literature summary extracted from

  • Faleev, N.G.; Zakomirdina, L.N.; Vorobev, M.M.; Tsvetikova, M.A.; Gogoleva, O.I.; Demidkina, T.V.; Phillips, R.S.
    A straightforward kinetic evidence for coexistence of induced fit and selected fit in the reaction mechanism of a mutant tryptophan indole lyase Y72F from Proteus vulgaris (2014), Biochim. Biophys. Acta, 1844, 1860-1867 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.1 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

EC Number Inhibitors Comment Organism Structure
4.1.99.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.99.1 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.1 L-tryptophan + H2O Proteus vulgaris
-
 indole + pyruvate + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.1 Proteus vulgaris P28796
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.1 L-tryptophan + H2O
-
 Proteus vulgaris indole + pyruvate + NH3
-
 ?
4.1.99.1 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 ?
-
 ?
4.1.99.1 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 ?
-
 ?
4.1.99.1 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

EC Number Synonyms Comment Organism
4.1.99.1 TIL
-
 Proteus vulgaris
4.1.99.1 tryptophan indole lyase
-
 Proteus vulgaris

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.1 25
-
 assay at Proteus vulgaris

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.99.1 7.8
-
 assay at Proteus vulgaris

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.1 pyridoxal 5'-phosphate dependent on Proteus vulgaris