. 2015 Jan 28;79(1):39–60. doi: 10.1128/MMBR.00031-14

TABLE 4.

Kinetic parameters of phenylalanine ammonia lyases/tyrosine ammonia lyases from different organisms toward l-phenylalanine and l-tyrosine

EC no.	Enzyme	Organism	Substrate	K_m (μM)	k_cat (s⁻¹)	k_cat/K_m (s⁻¹ M⁻¹)	Reference
4.3.1.24	Phenylalanine ammonia lyase	Rhodotorula rubra	l-Phe	446			157 ^a
4.3.1.24	Phenylalanine ammonia lyase	Rhodotorula rubra	l-Tyr	220			157 ^a
4.3.1.23	Tyrosine ammonia lyase	Saccharothrix espanaensis	l-Phe	2860	0.0038	1.3	154
	Tyrosine ammonia lyase	Saccharothrix espanaensis	l-Tyr	15.5	0.015	968	154
		Rhodobacter sphaeroides	l-Phe	560	0.01	18	170
		Rhodobacter sphaeroides	l-Tyr	60	0.02	333	170
		Rhodobacter capsulatus	l-Phe	560	0.04	57	170
		Rhodobacter capsulatus	l-Tyr	160	0.06	375	170
4.3.1.25	Phenylalanine/tyrosine ammonia lyase	Rhodotorula glutinis	l-Phe	183	1.6	8.7 × 10³	171 ^b
4.3.1.25	Phenylalanine/tyrosine ammonia lyase	Rhodotorula glutinis	l-Tyr	615	0.53	8.6 × 10²	171 ^b

k_cat and k_cat/K_m were not determined. However, the enzyme showed a V_max of 0.169 μmol min⁻¹ mg⁻¹ for l-Phe and 0.033 μmol min⁻¹ mg⁻¹ for l-Tyr.

Kinetic properties at pH 8.5. At pH 9.5 the RgTAL enzyme showed k_cat, K_m and k_cat/K_m values of 1.5 s⁻¹, 126 μM, and 1.2 × 10⁴ s⁻¹ M⁻¹, respectively, for l-Phe and 0.93 s⁻¹, 68 μM, and 1.4 × 10⁴ s⁻¹ M⁻¹, respectively, for l-Tyr.