4.3.1.24: phenylalanine ammonia-lyase
This is an abbreviated version!
For detailed information about phenylalanine ammonia-lyase, go to the full flat file.
Word Map on EC 4.3.1.24
-
4.3.1.24
-
phenol
-
phenylpropanoids
-
polyphenols
-
flavonoid
-
seedling
-
chalcone
-
elicitors
-
lignin
-
cinnamic
-
cultivar
-
4.3.1.5
-
anthocyanins
-
jasmonate
-
chitinase
-
postharvest
-
4-hydroxylase
-
trans-cinnamic
-
defense-related
-
p-coumaric
-
phytoalexins
-
pathogenesis-related
-
lignification
-
chlorogenic
-
phytophthora
-
petroselinum
-
parsley
-
4-coumarate
-
phenylketonuria
-
crispum
-
fresh-cut
-
elicitor-induced
-
wall-bound
-
dihydroflavonol
-
elicitor-treated
-
4-coumarate:coa
-
polyphenoloxidase
-
glutinis
-
4-reductase
-
rhodotorula
-
rhodosporidium
-
synthesis
-
3-o-glucosyltransferase
-
d-phenylalanine
-
pharmacology
-
dehydroalanine
-
medicine
-
hydroxycinnamoyl
-
monolignols
-
analysis
-
food industry
-
drug development
-
agriculture
-
syringyl
-
biotechnology
-
lindemuthianum
-
glycinea
-
matricaria
-
cinnamoyl-coa
-
nutrition
- 4.3.1.24
- phenol
-
phenylpropanoids
- polyphenols
- flavonoid
- seedling
- chalcone
- elicitors
- lignin
-
cinnamic
- cultivar
-
4.3.1.5
- anthocyanins
- jasmonate
- chitinase
-
postharvest
-
4-hydroxylase
-
trans-cinnamic
-
defense-related
-
p-coumaric
-
phytoalexins
-
pathogenesis-related
-
lignification
-
chlorogenic
- phytophthora
- petroselinum
- parsley
- 4-coumarate
- phenylketonuria
- crispum
-
fresh-cut
-
elicitor-induced
-
wall-bound
- dihydroflavonol
-
elicitor-treated
-
4-coumarate:coa
- polyphenoloxidase
- glutinis
-
4-reductase
- rhodotorula
- rhodosporidium
- synthesis
- 3-o-glucosyltransferase
- d-phenylalanine
- pharmacology
- dehydroalanine
- medicine
-
hydroxycinnamoyl
- monolignols
- analysis
- food industry
- drug development
- agriculture
-
syringyl
- biotechnology
- lindemuthianum
- glycinea
-
matricaria
- cinnamoyl-coa
- nutrition
Reaction
Synonyms
AtPAL 1, AtPAL 2, AtPAL 3, AtPAL 4, AtPAL-1, AtPAL-2, AtPAL-3, AtPAL-4, AtPAL2, AvPAL, DcPAL1, EC 4.3.1.5, EncP, L-phenylalanine ammonia-lyase, L-phenylalanine-ammonia lyase, LrPAL3, LsPAL1, More, PAL, PAL-CLEA, PAL1, PAL2, PAL3, PAL3a, PAL3b, PAL4, PAL5, PAL6, PALrs1, PcPAL1, Phe ammonia-lyase, phenylalanine ammonia lyase, phenylalanine ammonia-lyase, phenylalanine ammonia-lyase 1, phenylalanine ammonia-lyase 2, phenylalanine ammonia-lyase 3, phenylalanine ammonia-lyase 4, RgPAL, RxPAL, Sb04g026520, SsPAL1, TcPAL, ZmPAL2
ECTree
4.3.1.24 phenylalanine ammonia-lyaseAdvanced search results
results (
results (Engineering
Engineering on EC 4.3.1.24 - phenylalanine ammonia-lyase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F144H
F137A
-
mutation increased the activity significantly towards almost all non-natural analogues of phenylalanine compared to the wild-type enzyme. Moderate enhancement (15%) of the conversion in ammonia elimination from (4'-fluoro-[1,1'-biphenyl]-4-yl)alanine and for (5-phenylthiophen-2-yl)alanine (44%)
F137A/L138V
-
moderate enhancement (18%) of the conversion in ammonia elimination from (4'-fluoro-[1,1'-biphenyl]-4-yl)alanine and for (5-phenylthiophen-2-yl)alanine (48%)
F137V
F137V/I460V
-
moderate enhancement (39%) of the conversion in ammonia elimination from (4'-fluoro-[1,1'-biphenyl]-4-yl)alanine
I460A
-
mutation increased the activity significantly towards almost all non-natural analogues of phenylalanine compared to the wild-type enzyme, mutation decreases the Tm value significantly from 75°C to 51°C
I460V
-
mutation increased the activity significantly towards almost all non-natural analogues of phenylalanine compared to the wild-type enzyme
L137H
-
mutation almost doubles the kinetic D-isotope effect compared to wild-type enzyme
L137H/Q487E
-
mutation almost doubles the kinetic D-isotope effect compared to wild-type enzyme
Q487A
-
kinetic D isotope effect is of the same magnitude as wild-type enzyme
Y350F
-
kinetic D isotope effect is of the same magnitude as wild-type enzyme
V83A
-
mutant is more active than wild-type enzyme, turnover-number for L-Phe is 20.8fold higher than wild-type value, Km-value for L-Phe is 5.2fold higher than wild-type value
L108E
site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme
L108E/N458F
site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme
N458F
site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme
N458L
site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme
A88Q
the mutant enzyme produces 4-nitro-D-phenylalanine at a rate 2.82fold faster compared to the wild-type enzyme
C503S/C565S
E75A
-
shift of the pH optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 35% higher specific activity than that of the wild-type enzyme
E75L
-
shift of the pH optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 30% higher specific activity than that of the wild-type enzyme. The half-life of the mutant enzyme at 70°C is prolonged to 190 min from 130 min of the wild-type enzyme. The higher resistance to a low pH of 3.5 and protease make the mutant enzyme a candidate for oral medicine of phenylketonuria
E75Q
-
shift of the pH optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 24% higher specific activity than that of the wild-type enzyme. The half-life of the mutant enzyme at 70°C is prolonged to 180 min from 130 min of the wild-type enzyme
F18A
modest improvements in resistance against protease inactivation
H359K
the mutant enzyme produces 4-nitro-D-phenylalanine at a rate 3.34fold faster compared to the wild-type enzyme
H359Y
the mutant enzyme produces 4-nitro-D-phenylalanine at a rate 3.52fold faster compared to the wild-type enzyme
Q292C/C565S
R91K
-
the mutant shows increased activity compared to the wild-type enzyme
S263A
the mutant enzyme produces 4-nitro-D-phenylalanine at a rate 2.47fold faster compared to the wild-type enzyme
S456P
the mutant enzyme produces 4-nitro-D-phenylalanine at a rate 3.05fold faster compared to the wild-type enzyme
E75A
Trichormus variabilis FACHB-82
-
shift of the pH optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 35% higher specific activity than that of the wild-type enzyme
-
E75L
Trichormus variabilis FACHB-82
-
shift of the pH optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 30% higher specific activity than that of the wild-type enzyme. The half-life of the mutant enzyme at 70°C is prolonged to 190 min from 130 min of the wild-type enzyme. The higher resistance to a low pH of 3.5 and protease make the mutant enzyme a candidate for oral medicine of phenylketonuria
-
E75Q
Trichormus variabilis FACHB-82
-
shift of the pH optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 24% higher specific activity than that of the wild-type enzyme. The half-life of the mutant enzyme at 70°C is prolonged to 180 min from 130 min of the wild-type enzyme
-
additional information
F144H
decrease of activity with L-phenylalanine, increase of activity with L-tyrosine
F144H
-
marked reduction (30fold) in affinity for the substrate phenylalanine
F137V
-
mutation increased the activity significantly towards almost all non-natural analogues of phenylalanine compared to the wild-type enzyme
F137V
-
the mutant enzyme can transform L-styrylalanine with comparable activity to that of the wild-type enzyme with L-phenylalanine. Ammonia elimination from L-styrylalanine by the non-mutated wild-type enzyme takes place with a 777fold lower kcat/KM value than the deamination of the natural substrate, L-phenylalanine. The mutant enzyme shows enhanced catalytic efficiency in the ammonia elimination reaction of several racemic styrylalanine derivatives
C503S/C565S
-
site-directed mutagenesis, structure analysis and comparison to the wild-type enzyme, the mutant shows increased activity and resistance to proteases compared to the wild-type enzyme
C503S/C565S
-
the mutant shows high protein stability and is very efficient as protein therapeutics in treatment of phenylketonuria, PKU, with lowered phenylalanine levels in both vascular space and brain tissue over a 90 day trial period, resulting in reduced manifestations associated with PKU, including reversal of PKU-associated hypopigmentation and enhanced animal health in a mouse model, the wild-type enzyme is less efective, overview
C503S/C565S
reduced aggregation properties of the enzyme, without significantly altered enzyme activity
Q292C/C565S
Km and kcat similar to wild-type, specific activity increased in mutant compared to wild-type, T1/2 increased in mutant compared to wild-type
Q292C/C565S
displays more kinetic stability and chemical denaturation resistance
additional information
construction of a loss-of-function mutant DcPAL3 promoter-reporter construct and transient expression in protoplasts prepared from carrot suspension-cultured cells
additional information
-
construction of a loss-of-function mutant DcPAL3 promoter-reporter construct and transient expression in protoplasts prepared from carrot suspension-cultured cells
additional information
-
mutant lacking 21 N-terminal amino acids, no adverse effects on catalytic activity
additional information
a Tyr10-loop-in conformation of the enzyme structure is constructed by partial homology modeling, and the static and dynamic behavior of the loop-in/loop-out structures are compared
additional information
-
a Tyr10-loop-in conformation of the enzyme structure is constructed by partial homology modeling, and the static and dynamic behavior of the loop-in/loop-out structures are compared
additional information
-
building of Tyr-loop-in/loop-out model structure lacking the C-terminal domain
additional information
overexpression of the PALrs1 gene in Rhodiola sachalinensis plants results in a 3.3fold increase in 4-coumaric acid content, while levels of tyrosol and salidroside are 4.7fold and 7.7fold, respectively, lower in PALrs1 transgenic plants than in controls
additional information
-
overexpression of the PALrs1 gene in Rhodiola sachalinensis plants results in a 3.3fold increase in 4-coumaric acid content, while levels of tyrosol and salidroside are 4.7fold and 7.7fold, respectively, lower in PALrs1 transgenic plants than in controls
additional information
-
activity PAL encapsulated in cellulose nitrate microcapsules is only 23% of the activity of PAL in Tris buffer due to its incomplete encapsulation, optimzation of encapsulation method and efficiency, method, PAL activity free in the aqueous core of the microcapsules is 85.7% of the total activity in the homogenate of the microcapsules, while the activity of PAL bound to the membrane of the microcapsules is 14.3% of the total activity in the homogenate of the microcapsules, overview
additional information
-
building of Tyr-loop-in/loop-out model structure lacking the C-terminal domain
additional information
-
mutant lacking 21 N-terminal amino acids, no adverse effects on catalytic activity
additional information
-
development of an encapsulation method and optimzation of enzyme stability, overview
