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4.3.1.25: phenylalanine/tyrosine ammonia-lyase

This is an abbreviated version!
For detailed information about phenylalanine/tyrosine ammonia-lyase, go to the full flat file.

Word Map on EC 4.3.1.25

Reaction

L-phenylalanine
=
trans-cinnamate
 +
NH3

Synonyms

EC 4.3.1.5, PAL, PAL/TAL, PAL4, phenylalanine-tyrosine ammonia lyase, PTAL, RtPAL, Sb04g026510, Sb06g022740, SbPAL1

ECTree

     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.25 phenylalanine/tyrosine ammonia-lyase

Engineering

Engineering on EC 4.3.1.25 - phenylalanine/tyrosine ammonia-lyase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R123A
modest improvements in resistance against protease inactivation
R123H
modest improvements in resistance against protease inactivation
R123Q
modest improvements in resistance against protease inactivation
Y110A
modest improvements in resistance against protease inactivation
Y110H
modest improvements in resistance against protease inactivation
Y110L
modest improvements in resistance against protease inactivation
F102Y
the turnover rate for L-Tyr is improved 3.6fold, whereas the turnover rate for L-Phe is unaffected. Km values for both L-Tyr and L-Phe are increased by 7.6- and 24fold, respectively, which causes reduced enzyme efficiency for both substrates
H123F
the mutant shows 6.2fold elevation in catalytic efficiency (kcat/Km) for L-Phe, mainly due to a 5.7fold decrease in Km. The mutant enzyme loses activity for L-Tyr. The loss of polarity in the H123F mutant orients both L-Tyr and L-Phe in similar positions, where the ortho-carbon is closer to the methylidene carbon of 4-methylidene-imidazole-5-one
H123Y
the catalytic efficiency of the mutant enzyme for L-Phe is reduced, mainly due to a 10fold decrease in the turnover rate. The H123Y mutant also loses activity against L-Tyr
K443E
the mutant enzyme shows no measurable activity against any of the three substrates, L-Phe, L-Tyr, and L-His
Y96F
the mutant enzyme displays only trace amounts of activity for both L-Tyr and L-Phe