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EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Commentary	Reference
4.1.99.2	-999	-	more	-	33448, 33453
4.1.99.2	-999	-	more	pH-independent kinetic constants for substrates bearing small substituents	33467
4.1.99.2	-999	-	more	pre-steady state kinetics and steady state kinetic study, overview. TPL from Citrobacter freundii exhibits two basic pKas, with an average value of 7.8, in the pH dependence of kcat/Km, and kcat is pH-independent. The TPL reaction shows primary isotope effects of about 3 on kcat and 2 on kcat/Km for both enzymes, also suggesting that steps involving transfer of the alpha-proton are partially rate-limiting. The primary isotope effect increases to 5.4 and 3.8, respectively, for kcat and kcat/Km with alpha-[2H]-3-fluoro-L-tyrosine with H343A TPL, compared to 3.9 and 2.2 for wild-type TPL. Stopped-flow measurements, the reaction of TPL with L-tyrosine and 3-fluoro-L-tyrosine in the stopped-flow spectrophotometer also shows rapid formation of quinonoid intermediate	747245
4.1.99.2	-999	-	more	pre-steady-state kinetic and steady-state kinetics, kinetic analysis of recombinant wild-type and mutant enzymes, stopped-flow kinetics of enzyme mutant F448A	746580
4.1.99.2	-999	-	more	steady-state kinetics	746892
4.1.99.2	0.05	-	S-benzyl-L-Cys	mutant enzyme Y71F	33471
4.1.99.2	0.054	-	L-Tyr	-	33465
4.1.99.2	0.0915	-	L-Met	-	664834
4.1.99.2	0.1	-	3-fluoro-L-Tyr	wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C	678401
4.1.99.2	0.1	-	3-fluoro-L-Tyr	wild-type enzyme	33462

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Release 2023.1 (January 2023)