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(1,1'-biphenyl)acrylic acid + NH3
([1,1'-biphenyl]-4-yl)alanine
-
no product is detected with wild-type enzyme or either single mutants, 8% conversion with mutant enzyme F137A/I460V after 20 h
-
-
?
(2'-chloro-5-phenylthiophen-2-yl)acrylic acid + NH3
(2'-chloro-5-phenylthiophen-2-yl)alanine
-
no product is detected with wild-type enzyme or either single mutants, 2% conversion with mutant enzyme F137A/I460V after 20 h
-
-
?
(2'-chloro-5-phenylthiophen-2-yl)alanine
(2'-chloro-5-phenylthiophen-2-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
(2-phenylthiazol-4-yl)alanine
(2-phenylthiazol-4-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutant F137A provides low high conversion
-
-
?
(2E)-3-(1-benzofuran-2-yl)acrylic acid + NH3
2-amino-3-(1-benzofuran-2-yl)propanoic acid
-
-
-
-
r
(2E)-3-(1-benzothien-2-yl)acrylic acid + NH3
2-amino-3-(1-benzothien-2-yl)propanoic acid
-
-
-
-
r
(2E)-3-(2-furyl)acrylic acid + NH3
(S)-2-amino-3-(2-furyl)propanoic acid
-
-
-
-
r
(2E)-3-(2-thienyl)acrylic acid + NH3
2-amino-3-(2-thienyl)propanoic acid
-
-
-
-
r
(2E)-3-bromo-cinnamic acid + NH3
3-bromo-L-phenylalanine
112% compared to activity with trans-cinnamate
-
-
?
(2E)-3-fluoro-cinnamic acid + NH3
3-fluoro-L-phenylalanine
128% compared to activity with trans-cinnamate
-
-
?
(2E)-3-nitro-cinnamic acid + NH3
4-nitro-L-phenylalanine
54% compared to activity with trans-cinnamate
-
-
?
(2E)-4-amino-cinnamic acid + NH3
4-amino-L-phenylalanine
-
poor substrate
-
-
r
(2E)-4-bromo-cinnamic acid + NH3
4-bromo-L-phenylalanine
17% compared to activity with trans-cinnamate
-
-
?
(2E)-4-fluoro-cinnamic acid + NH3
4-fluoro-L-phenylalanine
(2E)-4-formyl-cinnamic acid + NH3
4-formyl-L-phenylalanine
-
-
-
-
r
(2E)-4-hydroxycinnamate + NH3
L-tyrosine
-
-
-
-
r
(2E)-4-methyl-cinnamic acid + NH3
4-methyl-L-phenylalanine
-
-
-
-
r
(2E)-4-nitro-cinnamic acid + NH3
4-nitro-L-phenylalanine
-
-
-
-
r
(2E)-4-trifluoromethyl-cinnamic acid + NH3
4-trifluoromethyl-L-phenylalanine
-
poor substrate
-
-
r
(2S)-2-amino-3-(3-fluorophenyl)propanoic acid
(2E)-3-(3-fluorophenyl)prop-2-enoic acid + NH3
-
-
-
r
(2S)-2-amino-3-(3-hydroxyphenyl)propanoic acid
(2E)-3-(3-hydroxyphenyl)prop-2-enoic acid + NH3
-
-
-
r
(2S)-2-amino-3-(4-fluorophenyl)propanoic acid
(2E)-3-(4-fluorophenyl)prop-2-enoic acid + NH3
-
-
-
r
(2S)-2-amino-3-(4-nitrophenyl)propanoic acid
(2E)-3-(4-nitrophenyl)prop-2-enoic acid + NH3
-
-
-
r
(2S)-2-amino-3-(pyridin-3-yl)propanoic acid
(2E)-3-(pyridin-3-yl)prop-2-enoic acid + NH3
-
-
-
r
(2S)-2-amino-3-(pyridin-4-yl)propanoic acid
(2E)-3-(pyridin-4-yl)prop-2-enoic acid + NH3
-
-
-
r
(2S)-2-amino-3-phenylpropanoic acid
(2E)-3-phenylprop-2-enoic acid + NH3
-
-
-
r
(2S)-2-amino-3-[4-(trifluoromethyl)phenyl]propanoic acid
(2E)-3-[4-(trifluoromethyl)phenyl]prop-2-enoic acid + NH3
-
-
-
r
(3-methoxy)alanine
(3-methoxy)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
(4'-chloro-5-phenylthiophen-2-yl)alanine
(4'-chloro-5-phenylthiophen-2-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
(4'-fluoro-[1,1'-biphenyl]-4-yl)acrylic acid + NH3
(4'-fluoro-[1,1'-biphenyl]-4-yl)alanine
-
no product is detected with wild-type enzyme or either single mutants, 6% conversion with mutant enzyme F137A/I460V after 20 h
-
-
?
(4'-fluoro-[1,1'-biphenyl]-4-yl)alanine
(4'-fluoro-[1,1'-biphenyl]-4-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion. 39% conversion with with mutant enzyme F137A/I460V, 18% conversion with mutant enzyme F137A/L138V, 15% conversion with mutant enzyme F137A
-
-
?
(5-phenylthiophen-2-yl)acrylic acid + NH3
(5-phenylthiophen-2-yl)alanine
-
no product is detected with wild-type enzyme or either single mutants, 6% conversion with mutant enzyme F137A/I460V after 20 h
-
-
?
(5-phenylthiophen-2-yl)alanine
(5-phenylthiophen-2-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion. 48% conversion with mutant enzyme F137A/L138V, 44% conversion with mutant enzyme F137
-
-
?
(E)-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
(E)-pent-2-ene-4-ynoate + NH3
L-propargylglycine
-
-
-
-
r
(naphthalen-2-yl)alanine
(naphthalen-2-yl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
(styryl)acrylic acid + NH3
(styryl)alanine
-
no product is detected with wild-type enzyme or either single mutants, but 22% and 27%, respectively, conversion can be achieved with the F137V/I460V and F137V/I460A double mutants
-
-
?
(styryl)alanine
(styryl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
([1,1'-biphenyl]-4-yl)alanine
(1,1'-biphenyl)acrylic acid + NH3
-
wild-type enzyme shows a very poor conversion even after long reaction times up to 48 h, mutants I460V and F137V and F137A provide medium to high conversion
-
-
?
2,3,4,5,6-pentafluoro-L-phenylalanine
2,3,4,5,6-pentafluoro-trans-cinnamate + NH3
-
-
-
r
2,6-difluoro-L-phenylalanine
2,6-difluoro-trans-cinnamate + NH3
-
-
-
r
2-amino-3-(1-benzofuran-2-yl)propanoic acid
(2E)-3-(1-benzofuran-2-yl)acrylic acid + NH3
-
49% of the rate with L-phenylalanine
-
-
r
2-amino-3-(1-benzothien-2-yl)propanoic acid
(2E)-3-(1-benzothien-2-yl)acrylic acid + NH3
-
14% of the rate with L-phenylalanine
-
-
r
2-amino-3-(2-furyl)propanoic acid
(2E)-3-(2-furyl)acrylic acid + NH3
-
34% of the rate with L-phenylalanine
-
-
r
2-amino-3-(2-thienyl)propanoic acid
(2E)-3-(2-thienyl)acrylic acid + NH3
-
101% of the rate with L-phenylalanine
-
-
r
2-amino-3-(3-thienyl)propanoic acid
(2E)-3-(3-thienyl)acrylic acid + NH3
-
16% of the rate with L-phenylalanine
-
-
r
2-chloro-L-phenylalanine
2-chloro-trans-cinnamate + NH3
-
-
-
r
2-chloro-trans-cinnamate + NH3
2-chloro-L-phenylalanine
2-fluoro-L-phenylalanine
2-fluoro-trans-cinnamate + NH3
-
-
-
r
2-fluoro-trans-cinnamate + NH3
2-fluoro-L-phenylalanine
2-hydroxy-trans-cinnamate + NH3
2-hydroxy-L-phenylalanine
2-methoxy-trans-cinnamate + NH3
2-methoxy-L-phenylalanine
3,4-dihydroxyphenylalanine
?
-
29% of the activity with L-Phe
-
-
?
3,5-difluoro-L-phenylalanine
3,5-difluoro-trans-cinnamate + NH3
-
-
-
r
3-chloro-L-phenylalanine
3-chloro-trans-cinnamate + NH3
3-chloro-trans-cinnamate + NH3
3-chloro-L-phenylalanine
3-fluoro-L-phenylalanine
3-fluoro-trans-cinnamate + NH3
-
-
-
r
3-fluoro-trans-cinnamate + NH3
3-fluoro-L-phenylalanine
3-hydroxy-trans-cinnamate + NH3
3-hydroxy-L-phenylalanine
3-methoxy-trans-cinnamate + NH3
3-methoxy-L-phenylalanine
4-chloro-L-phenylalanine
4-chloro-trans-cinnamate + NH3
-
-
-
?
4-chloro-trans-cinnamate + NH3
4-chloro-L-phenylalanine
4-fluoro-L-phenylalanine
4-fluoro-(E)-cinnamate + NH3
-
-
-
-
r
4-fluoro-L-phenylalanine
4-fluoro-trans-cinnamate + NH3
4-fluoro-trans-cinnamate + NH3
4-fluoro-L-phenylalanine
4-hydroxy-trans-cinnamate + NH3
4-hydroxy-L-phenylalanine
4-methoxy-trans-cinnamate + NH3
4-methoxy-L-phenylalanine
4-nitro-L-phenylalanine
4-nitro-(E)-cinnamate + NH3
-
-
-
-
r
4-nitro-trans-cinnamate + NH3
4-nitro-D-phenylalanine
-
-
-
?
4-nitro-trans-cinnamate + NH3
4-nitro-L-phenylalanine
-
-
-
?
4-trifluoromethyl-L-phenylalanine
4-trifluoromethyl-(E)-cinnamate + NH3
-
-
-
-
r
beta-(5-pyrimidinyl)-D,L-alanine
?
-
-
-
?
chlorophenylalanine
?
Streptomyces verticillatus
-
-
-
-
?
fluorophenylalanine
trans-(4-fluoro)cinnamate + NH3
L-Phe
(E)-cinnamate + NH3
L-phenylalanine
(E)-cinnamate + NH3
L-phenylalanine
trans-cinnamate + NH3
L-phenylalanine methyl ester
?
-
-
-
-
r
L-propargylglycine
(E)-pent-2-ene-4-ynoate + NH3
-
-
-
-
r
L-styrylalanine
(styryl)acrylic acid + NH3
-
-
-
-
?
L-Tyr
(2E)-4-hydroxycinnamate + NH3
L-Tyr
p-coumarate + NH3
-
-
-
?
L-tyrosine
(2E)-4-hydroxycinnamate + NH3
-
poor substrate
-
-
r
L-tyrosine
p-coumarate + NH3
L-tyrosine
trans-p-hydroxycinnamate + NH3
the enzyme is specific for L-phenylalanine, and shows low activity with L-tyrosine
-
-
?
N-methyl-L-phenylalanine
trans-cinnamate + methylamine
-
-
-
?
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
(2E,4E)-5-(4-chlorophenyl)penta-2,4-dienoic acid + NH3
-
-
-
-
?
rac-(E)-2-amino-5-phenylpent-4-enoic acid
(2E,4E)-5-phenylpenta-2,4-dienoic acid + NH3
-
-
-
-
?
trans-cinnamate + NH3
L-alpha-phenylalanine + L-beta-phenylalanine
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
trans-cinnamic acid + NH3
L-phenylalanine
additional information
?
-
(2E)-4-fluoro-cinnamic acid + NH3
4-fluoro-L-phenylalanine
-
-
-
-
r
(2E)-4-fluoro-cinnamic acid + NH3
4-fluoro-L-phenylalanine
109% compared to activity with trans-cinnamate
-
-
?
2-chloro-trans-cinnamate + NH3
2-chloro-L-phenylalanine
-
-
-
?
2-chloro-trans-cinnamate + NH3
2-chloro-L-phenylalanine
96.4% conversion
-
-
?
2-chloro-trans-cinnamate + NH3
2-chloro-L-phenylalanine
50.5% conversion
-
-
?
2-fluoro-trans-cinnamate + NH3
2-fluoro-L-phenylalanine
96.1% conversion
-
-
?
2-fluoro-trans-cinnamate + NH3
2-fluoro-L-phenylalanine
95.8% conversion
-
-
?
2-hydroxy-trans-cinnamate + NH3
2-hydroxy-L-phenylalanine
22.0% conversion
-
-
?
2-hydroxy-trans-cinnamate + NH3
2-hydroxy-L-phenylalanine
15.5% conversion
-
-
?
2-methoxy-trans-cinnamate + NH3
2-methoxy-L-phenylalanine
52.7% conversion
-
-
?
2-methoxy-trans-cinnamate + NH3
2-methoxy-L-phenylalanine
54.6% conversion
-
-
?
3-chloro-L-phenylalanine
3-chloro-trans-cinnamate + NH3
-
-
-
?
3-chloro-L-phenylalanine
3-chloro-trans-cinnamate + NH3
-
-
-
r
3-chloro-trans-cinnamate + NH3
3-chloro-L-phenylalanine
92.6% conversion
-
-
?
3-chloro-trans-cinnamate + NH3
3-chloro-L-phenylalanine
91.7% conversion
-
-
?
3-fluoro-trans-cinnamate + NH3
3-fluoro-L-phenylalanine
91.2% conversion
-
-
?
3-fluoro-trans-cinnamate + NH3
3-fluoro-L-phenylalanine
52.1% conversion
-
-
?
3-hydroxy-trans-cinnamate + NH3
3-hydroxy-L-phenylalanine
70.6% conversion
-
-
?
3-hydroxy-trans-cinnamate + NH3
3-hydroxy-L-phenylalanine
85.7% conversion
-
-
?
3-methoxy-trans-cinnamate + NH3
3-methoxy-L-phenylalanine
85.0% conversion
-
-
?
3-methoxy-trans-cinnamate + NH3
3-methoxy-L-phenylalanine
85.7% conversion
-
-
?
4-chloro-trans-cinnamate + NH3
4-chloro-L-phenylalanine
91.7% conversion
-
-
?
4-chloro-trans-cinnamate + NH3
4-chloro-L-phenylalanine
89.1% conversion
-
-
?
4-fluoro-L-phenylalanine
4-fluoro-trans-cinnamate + NH3
-
-
-
?
4-fluoro-L-phenylalanine
4-fluoro-trans-cinnamate + NH3
-
-
-
r
4-fluoro-trans-cinnamate + NH3
4-fluoro-L-phenylalanine
84.7% conversion
-
-
?
4-fluoro-trans-cinnamate + NH3
4-fluoro-L-phenylalanine
65.9% conversion
-
-
?
4-hydroxy-trans-cinnamate + NH3
4-hydroxy-L-phenylalanine
0.9% conversion
-
-
?
4-hydroxy-trans-cinnamate + NH3
4-hydroxy-L-phenylalanine
0.8% conversion
-
-
?
4-methoxy-trans-cinnamate + NH3
4-methoxy-L-phenylalanine
2.5% conversion
-
-
?
4-methoxy-trans-cinnamate + NH3
4-methoxy-L-phenylalanine
6.4% conversion
-
-
?
fluorophenylalanine
trans-(4-fluoro)cinnamate + NH3
-
p-fluorophenylalanine, 31% of the activity with L-Phe, o-fluorophenylalanine, 14% of the activity with L-Phe
-
-
?
fluorophenylalanine
trans-(4-fluoro)cinnamate + NH3
Streptomyces verticillatus
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
Clavaria cristata
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
Dunaliella marina
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
Fomes subroseus
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
no activity with D-Phe
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
cutting induces phenylalanine ammonia-lyase
-
-
?
L-Phe
(E)-cinnamate + NH3
-
the enzyme catalyzes the first step controlling the rate of phenylpropanoid metabolism, wound-inducible enzyme
-
-
?
L-Phe
(E)-cinnamate + NH3
Lupinus sp.
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
Polyporus adustus
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
Quercus pedunculata
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
Ramaria secunda
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
r
L-Phe
(E)-cinnamate + NH3
Rhodotorula texensis
-
-
-
?
L-Phe
(E)-cinnamate + NH3
mechanism: multiple helix dipoles implicated in catalysis
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
Steccherinum adustum
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
Streptomyces verticillatus
-
-
-
?
L-Phe
(E)-cinnamate + NH3
Streptomyces verticillatus
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
Xanthium pennsylvanicum
-
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
?
L-Phe
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
the enzyme catalyzes the first step in the biosynthetic pathway leading to calycosin-7-O-beta-D-glucoside, overview. Accumulation of mRNA for calycosin-7-O-beta-Dglucoside pathway genes during different temperature treatments
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
assay at pH 8.5, 37°C, reaction terminated by addition of HCl
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
first step in phenylpropanoid and flavonoid biosynthesis pathways, overview
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
a key enzyme in the synthesis of phenolic compounds, including phytoalexins, with anti-microbial antimicrobial properties that are important in the defence of plants
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
the enzyme is part of the plant's defense system, especially in the early stages of seed maturation
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
the enzyme is involved in the plant's defense system
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
first enzyme in the phenylpropanoid biosynthetic pathway
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
regulatory mechanism on PAL gene expression, overview
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
in ephedrine alkaloid biosynthesis in Ephedra, trans-cinnamic acid produced from a PAL reaction is converted into benzoic acid or benzoyl-CoA by beta-oxidation, branching off from the common phenylpropanoid pathway, biosynthetic pathway of ephedrine alkaloids, overview
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?, r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
assay at 40°C, pH 7.8
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
first step in flavonoid biosynthesis, the enzyme might have a regulatory role in flavonoid biosynthesis at transcriptional level
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?, r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
reaction can be reversed by applying high concentrations of ammonia
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
the enzyme is involved in the biosynthesis of salidroside, an effective adaptogenic drug extracted from the medicinal plant Rhodiola sachalinensis, two different possible biosynthetic pathways via tyrosol, overview
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
the enzyme catalyzes the reverse reaction from a 2% trans-cinnamic acid with (NH4)2SO4 solution
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
the enzyme catalyzes the reverse reaction from a 2% trans-cinnamic acid with (NH4)2SO4 solution
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?, r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
Ala-Ser-Gly triad
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?, r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
phenylalanine ammonia-lyase is an important enzyme in both plant development and pathogen defense
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
PAL is a key enzyme in plant stress responses
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?, r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
phenylalanine ammonia-lyase is the first enzyme in the phenylpropanoid pathway catalyzing monooxidative deamination of phenylalanine to produce cinnamate, overview
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
key enzyme in phenylpropanoid metabolism of grape berry
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
the enzyme is involved in phenylpropanoid biosynthesis
-
-
?
L-phenylalanine
trans-cinnamate + NH3
the enzyme is specific for L-phenylalanine, and shows low activity with L-tyrosine
-
-
?
L-phenylalanine
trans-cinnamate + NH3
no activity with L-Tyr or L-His
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
Coleus scutellarioides
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
Coleus scutellarioides
the enzyme is involved in the phenylpropanoid pathway and plays important roles in the secondary metabolisms, development and defense of plants
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
no activity with L-Tyr or L-His
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
enzyme of the plant phenylpropanoid pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
the enzyme is involved in the biosynthesis of galanthamine
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
no activity with L-Tyr or L-His
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
reversibility of the reaction is demonstrated for the natural substrate L-Phe at an ammonium carbonate concentration as low as 0.1 M
-
-
r
L-phenylalanine
trans-cinnamate + NH3
the enzyme is specific for L-phenylalanine
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
no activity with L-Tyr or L-His
-
-
?
L-phenylalanine
trans-cinnamate + NH3
no activity with L-Tyr or L-His
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
enzyme of the phenylpropanoid pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
no activity with L-Tyr or L-His
-
-
?
L-phenylalanine
trans-cinnamate + NH3
Streptomyces verticillatus
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
Streptomyces verticillatus
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
no activity with L-Tyr or L-His
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
MG745168
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
MG745168
enzyme of the phenylpropanoid pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
MG745168
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
MG745168
enzyme of the phenylpropanoid pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
the recombinant ZmPAL2 exhibits a high phenylalanine ammonia-lyase activity (7.14 U/mg) and a weak tyrosine ammonia-lyase activity
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
rate-limiting enzyme of phenolic biosynthetic pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
rate-limiting enzyme of phenolic biosynthetic pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
rate-limiting enzyme of phenolic biosynthetic pathway
-
-
?
L-Tyr
(2E)-4-hydroxycinnamate + NH3
poor substrate
-
-
?
L-Tyr
(2E)-4-hydroxycinnamate + NH3
-
-
-
?
L-tyrosine
p-coumarate + NH3
-
-
-
?
L-tyrosine
p-coumarate + NH3
-
no activity
-
-
?
L-tyrosine
p-coumarate + NH3
-
no activity
-
-
?
L-tyrosine
p-coumarate + NH3
-
L-Tyr
-
-
?
L-tyrosine
p-coumarate + NH3
-
no activity
-
-
?
L-tyrosine
p-coumarate + NH3
-
m-Tyr, 10% of the activity with L-Phe
-
-
?
L-tyrosine
p-coumarate + NH3
-
L-Tyr, 15% of the activity with L-Phe
-
-
?
L-tyrosine
p-coumarate + NH3
-
-
-
-
?
L-tyrosine
p-coumarate + NH3
-
no activity
-
-
?
L-tyrosine
p-coumarate + NH3
-
no activity
-
-
?
L-tyrosine
p-coumarate + NH3
Streptomyces verticillatus
-
no activity
-
-
?
L-tyrosine
p-coumarate + NH3
-
poor substrate
-
-
?
L-tyrosine
p-coumarate + NH3
-
no activity
-
-
?
L-tyrosine
p-coumarate + NH3
-
no deamination of L-Tyr
-
-
?
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
89.6% conversion
-
-
?
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
?
trans-cinnamate + NH3
L-phenylalanine
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
85.2% conversion
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
?
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
?
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
Streptomyces verticillatus
-
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
r
trans-cinnamate + NH3
L-phenylalanine
-
-
-
-
r
trans-cinnamic acid + NH3
L-phenylalanine
Rhodococcus rubra
-
-
-
-
?
trans-cinnamic acid + NH3
L-phenylalanine
-
-
-
-
?
additional information
?
-
-
key enzyme in the formation of a variety of phenolic compounds
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
phenylalanine ammonia lyase PAL1 functions as a switch directly controlling the accumulation of calycosin and calycosin-7-O-beta-D-glucoside in Astragalus membranaceus var. mongholicus plants by limiting the compound levels in a light-dependent manner during low temperature treatment, overview
-
-
?
additional information
?
-
-
phenylalanine ammonia lyase PAL1 functions as a switch directly controlling the accumulation of calycosin and calycosin-7-O-beta-D-glucoside in Astragalus membranaceus var. mongholicus plants by limiting the compound levels in a light-dependent manner during low temperature treatment, overview
-
-
?
additional information
?
-
-
enzyme may be involved in detoxification of Cd2+
-
-
?
additional information
?
-
-
L-Tyr is a poor substrate
-
-
?
additional information
?
-
L-Tyr is a poor substrate
-
-
?
additional information
?
-
no substrate: L-Tyr
-
-
?
additional information
?
-
no substrate: L-Tyr
-
-
?
additional information
?
-
no substrate: L-Tyr
-
-
?
additional information
?
-
-
no substrate: L-Tyr
-
-
?
additional information
?
-
-
first enzyme in phenylpropanoid biosynthesis
-
-
?
additional information
?
-
-
first enzyme in phenylpropanoid biosynthesis
-
-
?
additional information
?
-
the core reactions of phenylpropanoid metabolism involve three enzymes, phenylalanine ammonia-lyase, cinnamate 4-hydroxylase, and 4-coumarate coenzyme A ligase, pathway, overview
-
-
?
additional information
?
-
-
the core reactions of phenylpropanoid metabolism involve three enzymes, phenylalanine ammonia-lyase, cinnamate 4-hydroxylase, and 4-coumarate coenzyme A ligase, pathway, overview
-
-
?
additional information
?
-
no substrate: L-Tyr
-
-
?
additional information
?
-
-
no substrate: L-Tyr
-
-
?
additional information
?
-
-
UV-B light induces a single PAL isoform, which plays an important role in the regulation of the biosynthesis of phenylpropanoid metabolites
-
-
?
additional information
?
-
-
no substrate: 2-amino-3-(3-furyl)propanoic acid. Enzyme acts selectively on L-amino acids and their derivatives
-
-
?
additional information
?
-
-
the 83000 Da enzyme form may be constitutive and involved in the low-level accumulation of phenolics in most cell types, the 77000 Da enzyme form is rapidly induced during elicitor action, wounding or cytokinin-induced xylogenesis as a key regulatory enzyme involved in the synthesis of phenolics under stress conditions or during differentiation
-
-
?
additional information
?
-
-
the enzyme is involved in the lignification of pine suspension cultures in response to an elicitor prepared from an extomycorrhizal fungus
-
-
?
additional information
?
-
-
among the water miscible solvents, ethanol treated and methanol treated enzymes supported maximum PAL forward and reverse activities, respectively. In the water immiscible solvents category, heptane-treated enzyme exhibits maximal activity for both PAL forward and reverse reactions
-
-
?
additional information
?
-
-
enzyme shows a higher affinity towards substrate L-tyrosine compared to L-phenylalanine
-
-
?
additional information
?
-
-
3 isoforms, which are differentially induced and affected by metabolites belonging to particular branches of phenylpropanoid pathway
-
-
?
additional information
?
-
PAL activity seems to be extraordinarily sensitive to the physiological state of the plant
-
-
?
additional information
?
-
-
PAL activity seems to be extraordinarily sensitive to the physiological state of the plant
-
-
?
additional information
?
-
-
key enzyme of phenylpropanoid metabolism
-
-
?
additional information
?
-
TcPAM catalyzes the isomerization of alpha-phenylalanine to beta-phenylalanine through exchanging the position of the amine group (Calpha -> Cbeta) and pro-3S hydrogen proton (Cbeta -> Calpha) with retention of the configuration at the reaction termini, which requires reorientation after deamination of L-phenylalanine to trans-cinnamic acid in which the reface of the Cbeta and the si-face of the Cbeta carton atoms are positioned for amine readdition and reprotonation. The enzyme TcPAM (EC 5.4.3.10) also catalyzes the regioselective hydroamination of transcinnamic acid (t-CA) to yield L-beta-Phe, TcPAL. The final product mixture consists of both alpha- and beta-Phe owing to low regioselectivity of the enzyme. Substrate docking
-
-
?
additional information
?
-
-
no substrate: L-histidine
-
-
?
additional information
?
-
-
structure-function relationship, with helix-loop conformational switch, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-Phe
(E)-cinnamate + NH3
L-phenylalanine
(E)-cinnamate + NH3
L-phenylalanine
trans-cinnamate + NH3
trans-cinnamate + NH3
L-phenylalanine
-
-
-
r
additional information
?
-
L-Phe
(E)-cinnamate + NH3
-
cutting induces phenylalanine ammonia-lyase
-
-
?
L-Phe
(E)-cinnamate + NH3
-
the enzyme catalyzes the first step controlling the rate of phenylpropanoid metabolism, wound-inducible enzyme
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
the enzyme catalyzes the first step in the biosynthetic pathway leading to calycosin-7-O-beta-D-glucoside, overview. Accumulation of mRNA for calycosin-7-O-beta-Dglucoside pathway genes during different temperature treatments
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
first step in phenylpropanoid and flavonoid biosynthesis pathways, overview
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
a key enzyme in the synthesis of phenolic compounds, including phytoalexins, with anti-microbial antimicrobial properties that are important in the defence of plants
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
the enzyme is part of the plant's defense system, especially in the early stages of seed maturation
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
the enzyme is involved in the plant's defense system
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
first enzyme in the phenylpropanoid biosynthetic pathway
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
regulatory mechanism on PAL gene expression, overview
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
in ephedrine alkaloid biosynthesis in Ephedra, trans-cinnamic acid produced from a PAL reaction is converted into benzoic acid or benzoyl-CoA by beta-oxidation, branching off from the common phenylpropanoid pathway, biosynthetic pathway of ephedrine alkaloids, overview
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
first step in flavonoid biosynthesis, the enzyme might have a regulatory role in flavonoid biosynthesis at transcriptional level
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
the enzyme is involved in the biosynthesis of salidroside, an effective adaptogenic drug extracted from the medicinal plant Rhodiola sachalinensis, two different possible biosynthetic pathways via tyrosol, overview
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
phenylalanine ammonia-lyase is an important enzyme in both plant development and pathogen defense
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
PAL is a key enzyme in plant stress responses
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
-
-
-
r
L-phenylalanine
(E)-cinnamate + NH3
-
phenylalanine ammonia-lyase is the first enzyme in the phenylpropanoid pathway catalyzing monooxidative deamination of phenylalanine to produce cinnamate, overview
-
-
?
L-phenylalanine
(E)-cinnamate + NH3
key enzyme in phenylpropanoid metabolism of grape berry
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
the enzyme is involved in phenylpropanoid biosynthesis
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
Coleus scutellarioides
the enzyme is involved in the phenylpropanoid pathway and plays important roles in the secondary metabolisms, development and defense of plants
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
enzyme of the plant phenylpropanoid pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
the enzyme is involved in the biosynthesis of galanthamine
-
-
?
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
enzyme of the phenylpropanoid pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
Streptomyces verticillatus
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
-
-
r
L-phenylalanine
trans-cinnamate + NH3
-
-
-
?
L-phenylalanine
trans-cinnamate + NH3
MG745168
enzyme of the phenylpropanoid pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
MG745168
enzyme of the phenylpropanoid pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
rate-limiting enzyme of phenolic biosynthetic pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
rate-limiting enzyme of phenolic biosynthetic pathway
-
-
?
L-phenylalanine
trans-cinnamate + NH3
-
rate-limiting enzyme of phenolic biosynthetic pathway
-
-
?
additional information
?
-
-
key enzyme in the formation of a variety of phenolic compounds
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purification-mass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
-
Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes (PAL1, PAL2, PAL3, PAL4) as shown in a yeast-two-hybrid system and tandem affinity protein purificationmass spectrometry
-
-
?
additional information
?
-
phenylalanine ammonia lyase PAL1 functions as a switch directly controlling the accumulation of calycosin and calycosin-7-O-beta-D-glucoside in Astragalus membranaceus var. mongholicus plants by limiting the compound levels in a light-dependent manner during low temperature treatment, overview
-
-
?
additional information
?
-
-
phenylalanine ammonia lyase PAL1 functions as a switch directly controlling the accumulation of calycosin and calycosin-7-O-beta-D-glucoside in Astragalus membranaceus var. mongholicus plants by limiting the compound levels in a light-dependent manner during low temperature treatment, overview
-
-
?
additional information
?
-
-
enzyme may be involved in detoxification of Cd2+
-
-
?
additional information
?
-
-
first enzyme in phenylpropanoid biosynthesis
-
-
?
additional information
?
-
-
first enzyme in phenylpropanoid biosynthesis
-
-
?
additional information
?
-
the core reactions of phenylpropanoid metabolism involve three enzymes, phenylalanine ammonia-lyase, cinnamate 4-hydroxylase, and 4-coumarate coenzyme A ligase, pathway, overview
-
-
?
additional information
?
-
-
the core reactions of phenylpropanoid metabolism involve three enzymes, phenylalanine ammonia-lyase, cinnamate 4-hydroxylase, and 4-coumarate coenzyme A ligase, pathway, overview
-
-
?
additional information
?
-
-
UV-B light induces a single PAL isoform, which plays an important role in the regulation of the biosynthesis of phenylpropanoid metabolites
-
-
?
additional information
?
-
-
the 83000 Da enzyme form may be constitutive and involved in the low-level accumulation of phenolics in most cell types, the 77000 Da enzyme form is rapidly induced during elicitor action, wounding or cytokinin-induced xylogenesis as a key regulatory enzyme involved in the synthesis of phenolics under stress conditions or during differentiation
-
-
?
additional information
?
-
-
the enzyme is involved in the lignification of pine suspension cultures in response to an elicitor prepared from an extomycorrhizal fungus
-
-
?
additional information
?
-
-
3 isoforms, which are differentially induced and affected by metabolites belonging to particular branches of phenylpropanoid pathway
-
-
?
additional information
?
-
PAL activity seems to be extraordinarily sensitive to the physiological state of the plant
-
-
?
additional information
?
-
-
PAL activity seems to be extraordinarily sensitive to the physiological state of the plant
-
-
?
additional information
?
-
-
key enzyme of phenylpropanoid metabolism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(+)-1-amino-3',4'-dichlorobenzylphosphonic acid
-
strongest inhibitor among 1-aminobenzylphosphonic acids
(+-)-2-aminomethyl-3-phenylpropanoic acid
-
-
(+-)-2-aminooxy-3-phenylpropanoic acid
-
strong inhibition
(2-amino-2,3-dihydro-1H-inden-2-yl)phosphonic acid
-
powerful inhibitor
(2S)-2-amino-3-(1-benzofuran-3-yl)propanoic acid
-
competitive
(2S)-2-amino-3-(1-benzothien-3-yl)propanoic acid
-
competitive
(R)-1-amino-2-(4-fluorophenyl)ethylphosphonic acid
-
-
(R)-1-amino-2-phenylethylphosphonic acid
-
-
(R)-1-amino-2-phenylwthylphosphonic acid
-
strong inhibition
(S)-2-aminooxy-3-phenylpropanoic acid
(S)-2-aminooxy-3-phenylpropionic acid
-
-
1-amino-2-phenylethyl-phosphonic acid
1-amino-3-phenylpropylphosphonate
-
inhibitory effect is half of that of 1-amino-2-phenylethyl-phosphonic acid
1-aminobenzocyclobutene-1-phosphonic acid
-
six times weaker than the inhibitor 1-aminobenzocyclobutene-1-phosphonic acid
1-aminobenzylphosphonic acid
-
various substitutes in the benzene ring
2-amino-3-(1-benzofuran-3-yl)propanoic acid
-
competitive
2-amino-3-(1-benzothien-3-yl)propanoic acid
-
competitive
2-amino-4-bromoindane-2-phosphonic acid
-
-
2-amino-4-hydroxyindane-2-phosphonic acid
-
-
2-aminoindan-2-carboxylic acid
-
-
2-aminoindan-2-phosphonic acid
2-aminoindane-2-phosphonate
2-aminoindane-2-phosphonic acid
2-methoxy-cinnamaldehyde
-
0.010 mg/ml, 82% inhibition; 0.010 mg/ml, complete inhibition
2-phenyl-4,4,5,5-tetramethyl-imidazoline-1-oxyl-3-oxide
-
partially blocks PAL activity in immobilized cells
3,4-dihydroxybenzoate
-
-
3,4-dihydroxycinnamic acid
-
-
3,4-dihydroxyphenyl-DL-Ala
-
-
3-phenylpropionaldehyde
-
0.010 mg/ml, 67% inhibition
4-hydroxy-3-methoxycinnamic acid
-
-
4-hydroxycinnamic acid
-
-
ADP
-
5 mM, approx. 50% inhibition
AMP
-
5 mM, approx. 40% inhibition
ATP
-
5 mM, approx. 80% inhibition
benzoate
-
uncompetitive inhibition of enzyme form PAL68, non-competitive inhibition of enzyme form PAL116
beta-(2-pyrimidinyl)-D,L-alanine
-
competitive inhibition
beta-chloroethyltrimethylammonium
-
10 mM, 60% inhibition of PAL activity in cotyledons
beta-phenylethylamine
-
-
Cd2+
-
CdCl2, 1 mM, 100% inhibition
coniferyl alcohol
competitive
coniferyl aldehyde
competitive
coumaric acid
uncompetitive
EDTA
-
35 mM, complete inactivation
Fe2+
1 mM, about 20% loss of activity
heptakis(2,3,6-tri-O-methyl)cyclomaltoheptaose
-
-
heptakis(2,3-di-O-methyl)cyclomaltoheptaose
-
competitive and noncompetitive inhibition
hexakis(2,3,6-tri-O-methyl)cyclomaltohexaose
-
-
hexakis(2,3-di-O-methyl)cyclomaltohexaose
-
competitive and noncompetitive inhibition, activation at 2 and 3 mM
His
Streptomyces verticillatus
-
-
indole butyric acid
at concentrations higher than 0.001 mM there is inhibitory effect on PAL specific activity
K+
1 mM, 1% loss of activity
kaempferol
-
mixed inhibition
L-2-aminooxy-3-phenylpropionic acid
-
-
L-alpha-aminooxy-beta-phenylpropionic acid
N,N-Dicyclohexylcarbodiimide
-
10 mM, 82% inhibition
N,N-dimethyl-4-nitro-L-phenylalanine
-
-
N-acetylimidazol
-
10 mM, 75% inhibition
N-methyl-4-nitro-L-phenylalanine
-
-
Nomega-Nitro-L-arginine
-
partially blocks PAL activity in immobilized cells
o-hydroxy-trans-cinnamic acid
-
-
o-phenanthroline
-
20 mM, complete inactivation
p-chloromercuriphenylsulfonic acid
-
-
Pb2+
1 mM, 50% loss of activity
Phenylmethylsulphonyl fluoride
-
10 mM, 59% inhibition
salicylic acid
-
PAL activity decreases with prolonged exposure to 0.25 mM salicylic acid indicating its inhibition
scopoletin
-
increases the negative cooperativity between the substrate binding sites
trans-cinnamaldehyde
-
0.010 mg/ml, complete inhibition
trans-cinnamate
product inhibition, 1.4 mM, about 40% loss of activity
trans-cinnamic acid
-
product inhibition, PAL is tightly regulated by a feedback mechanism
umbelliferone
-
increases the negative cooperativity between the substrate binding sites
(S)-2-aminooxy-3-phenylpropanoic acid
-
-
(S)-2-aminooxy-3-phenylpropanoic acid
-
very strong inhibition
1-amino-2-phenylethyl-phosphonic acid
-
(R)-1-amino-2-phenylethyl-phosphonic acid
1-amino-2-phenylethyl-phosphonic acid
-
-
2-aminoindan-2-phosphonic acid
competitive, specific inhibitor
2-aminoindan-2-phosphonic acid
-
-
2-aminoindan-2-phosphonic acid
-
strongly inhibits PAL activity, such that PAL activity is reduced to about 48.2% of the control level at 9 days of storage at 8°C
2-aminoindan-2-phosphonic acid
-
-
2-aminoindan-2-phosphonic acid
-
-
2-aminoindane-2-phosphonate
-
-
2-aminoindane-2-phosphonate
-
-
2-aminoindane-2-phosphonate
-
-
2-aminoindane-2-phosphonic acid
-
-
2-aminoindane-2-phosphonic acid
-
inhibition of browning reaction of cut lettuce at 0.01 mM
2-mercaptoethanol
competitive inhibition; competitive inhibition; competitive inhibition; competitive inhibition
2-mercaptoethanol
-
slight
2-mercaptoethanol
-
above 25 mM
4-coumarate
-
inhibition of enzyme form PAL116, no inhibition of enzyme form PAL68
4-coumarate
-
trans-p-coumarate, competitive
4-coumarate
-
0.1 mM, slight
aminooxyacetic acid
-
-
aminooxyacetic acid
-
a reduction in PAL activity is observed in hairy roots, supplemented with 0.5-1 mM aminooxyacetic acid
aminooxyacetic acid
-
irreversible inhibition, treatment results in decrease in content of 2-hydroxy-4-methoxybenzaldehyde
Ca2+
-
1 mM, 20% inhibition
Ca2+
-
6 mM, 40% inhibition
Ca2+
-
CaCl2, 1 mM, 57% inhibition
Ca2+
1 mM, about 5% loss of activity
caffeate
-
-
caffeate
-
0.1 mM, slight
chlorogenic acid
uncompetitive
Cinnamic acid
-
enzyme form PAL116 is inhibited, no inhibition of enzyme form PAL68
Cinnamic acid
-
trans-cinnamate does not inhibit
Cinnamic acid
-
competitive; trans-cinnamic acid
Cinnamic acid
-
trans-cinnamic acid
Cinnamic acid
-
(E)-cinnamate, competitive
Cinnamic acid
-
0.1 mM, slight
Cinnamic acid
Streptomyces verticillatus
-
-
Cinnamic acid
-
trans-cinnamate, moderately; trans-cinnamic acid
cinnamyl alcohol
uncompetitive
CN-
-
KCN, 1 mM, 85% inhibition
CN-
Streptomyces verticillatus
-
irreversible
Co2+
-
strong inhibition
Co2+
1 mM, 17% loss of activity
Cu2+
-
1 mM, 33% inactivation
Cu2+
-
CuSO4, 1 mM, 18% inactivation
Cu2+
1 mM, about 50% loss of activity
Cu2+
1 mM, 51% loss of activity
D-Phe
-
-
D-phenylalanine
-
competitive inhibition
D-phenylalanine
competitive inhibition
Fe3+
1 mM, about 10% loss of activity
ferulate
-
-
fluorophenylalanine
-
-
fluorophenylalanine
Streptomyces verticillatus
-
-
gallic acid
-
mixed inhibition
GSH
-
-
Hg2+
1 mM, 65% loss of activity
Hg2+
-
HgCl2, 0.01 mM, 100% inhibition
L-alpha-aminooxy-beta-phenylpropionic acid
-
-
L-alpha-aminooxy-beta-phenylpropionic acid
-
L-Cys
-
-
Mn2+
1 mM, about 10% loss of activity
Mn2+
1 mM, 21% loss of activity
Na+
1 mM, about 20% loss of activity
Na+
1 mM, 3% loss of activity
NaBH4
-
irreversible
NaBH4
Streptomyces verticillatus
-
irreversible
o-coumarate
-
competitive
p-chloromercuribenzoate
-
slight
p-chloromercuribenzoate
-
-
p-hydroxybenzoate
-
inhibition of enzyme form PAL116, no inhibition of enzyme form P68
quercetin
-
mixed inhibition
Tyr
-
competitive; L-Tyr
Zn2+
-
1 mM, complete inhibition
Zn2+
1 mM, 65% loss of activity
Zn2+
-
ZnSO4, 1 mM, 32% inhibition
Zn2+
1 mM, about 80% loss of activity
Zn2+
1 mM, 70% loss of activity
additional information
the plant hormones abscisic acid and gibberellic acid GA3 or drought stress lead to downregulation of PAL within several days
-
additional information
-
the plant hormones abscisic acid and gibberellic acid GA3 or drought stress lead to downregulation of PAL within several days
-
additional information
infections with pathogen Nacobbus aberrans alone or in combination with Phytophthora capsici suppress the enzyme expression in strain CM-334 leading to a reduction of enzyme activity by 48% after 21 days, overview
-
additional information
not inhibitory: tyrosol, caffeic acid
-
additional information
-
not inhibitory: tyrosol, caffeic acid
-
additional information
DcPAL3 promoter activity is strongly repressed by 2,4-dichlorophenoxyacetic acid
-
additional information
-
DcPAL3 promoter activity is strongly repressed by 2,4-dichlorophenoxyacetic acid
-
additional information
-
heat-shock treatment with chlorinated water and ascorbic acid, or with chlorinated water and CaCl2 reduces the enzyme activity, stronger reduction with the latter variant, effects of timing of the treatment before or immediately after cutting, overview
-
additional information
-
cyclodextrins show mixed inhibition, both competitive and noncompetitive, but they also act as activators for selected concentrations. The inhibitory effect of cyclodextrins is connected with the decrease of substrate concentration and unfavourable influence on the flexibility of the enzyme molecules. On the other hand, the activating effect is connected with the decrease of product concentration i.e. the product is an inhibitor of the enzymatic reaction under investigation
-
additional information
-
putative non-diffusible inhibitor
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
abscisic acid
-
exogenous application of abscisic acid (up to 0.08 mM) enhances PAL activity
Cd2+
-
treatment with Cd2+ results in increase in enzyme activitiy along with increase in total phenolics content and decrease in content of chlorophyll and carotinoids in the fronds
cetyl trimethyl ammonium bromide
8.2fold
chitosan
-
treatment leads to increased enzymic activity in cortex and cork tissues, with maximum specific activity after 12 h, and accumulation of phenolic compounds including 2-hydroxy-4-methoxybenzaldehyde
fluridone
-
effective in increase of PAL activity
jasmonic acid
-
jasmonic acid addition enhances PAL activity
L-phenylalanine
-
exposure of 4-week old plants to phenylalanine increases enzyme activity as well as accumulation of coumarin-related compounds
L-tyrosine
-
exposure of 4-week old plants to L-tyrosine at 0.01 or 0.1 mM significantly increases enzyme activity and increases free tyrosine content, while free phenylalanine content decreases. Tyrosine has no effect on coumarin accumulation
NaCl
-
maximal activity at 200 mM, inhibition above
phytotoxic protein
-
phytotoxic protein PcF from Phytophthora cactorum induces PAL activity in seedlings
-
S-methyl 1,2,3-benzothiadiazole-7-carbothioate
-
treatment of fruits
salicylic acid
activates phenylalanine ammonia-lyase in grape berry in response to high temperature stress, it also induces the accumulation of PAL mRNA and the synthesis of new PAL protein, in addition to increasing the enzyme activity, under high temperature stress
2-mercaptoethanol
-
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
2-mercaptoethanol
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
ascorbic acid
-
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
ascorbic acid
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
caffeate
-
strong activation
caffeate
-
strong activation
EDTA
-
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
EDTA
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
additional information
accumulation of mRNA for calycosin-7-O-beta-D-glucoside pathway genes during different temperature treatments
-
additional information
-
accumulation of mRNA for calycosin-7-O-beta-D-glucoside pathway genes during different temperature treatments
-
additional information
-
the enzyme activity is stimulated by chilling, wounding, UV-B light, ozone, pathogen invasion, and plant hormones
-
additional information
-
treatment of plants with Pseudomonas fluorescens and Pseudomonas aeruginosa induces enzyme synthesis associated with increased synthesis of phenolic compounds such as tannic, gallic, caffeic, chlorogenic and cinnamic acids. Treatment with Sclerotinia slerotiorum does not induce enzyme synthesis
-
additional information
-
infection with Bemisia tabaci strongly induces the enzyme in cucumber with a first high activity peak by 23.1% at 6 h after infection and the highest activitypeak by 29.1% at 48 h after infection compared to the control
-
additional information
transcriptional activation by binding of DcERF1, but not by DcERF2. The trans-activating factors DcERF1 and DcERF2, ethylene-responsive element-binding factors, to the GCC-box homolog sequence, specifically interact with the promoter region, binding specificity, overview. DcERF2 can function as a transcriptional activator when it is localized in the nucleus of carrot protoplasts
-
additional information
-
transcriptional activation by binding of DcERF1, but not by DcERF2. The trans-activating factors DcERF1 and DcERF2, ethylene-responsive element-binding factors, to the GCC-box homolog sequence, specifically interact with the promoter region, binding specificity, overview. DcERF2 can function as a transcriptional activator when it is localized in the nucleus of carrot protoplasts
-
additional information
transcriptional activation by binding of DcERF1, but not by DcERF2. The trans-activating factors DcERF1 and DcERF2, ethylene-responsive element-binding factors, to the GCC-box homolog sequence, specifically interact with the promoter region, binding specificity, overview. The full DcPAL3 promoter abolishes the upregulation ability of DcERF1. DcERF2 can function as a transcriptional activator when it is localized in the nucleus of carrot protoplasts
-
additional information
-
transcriptional activation by binding of DcERF1, but not by DcERF2. The trans-activating factors DcERF1 and DcERF2, ethylene-responsive element-binding factors, to the GCC-box homolog sequence, specifically interact with the promoter region, binding specificity, overview. The full DcPAL3 promoter abolishes the upregulation ability of DcERF1. DcERF2 can function as a transcriptional activator when it is localized in the nucleus of carrot protoplasts
-
additional information
the enzyme is induced by various stresses, e.g. by UV-B light, wounding, cold, and salicylic acid
-
additional information
-
heat treatment at 38°C for 3 days induces accumulation of PAL protein
-
additional information
induction by the combination of L-phenylalanine and L-tyrosine, Ethanol, isopropyl alcohol and chloroform fail to enhance PAL activity significantly
-
additional information
red light, acting via phytochrome, stimulates phenylalanine ammonia lyase activity in cotyledons and hypocotyls of tomato seedlings in a manner dependent on de novo synthesis of protein and nucleic acid. Photostimulation of PAL activity likely requires dephosphorylation by a type 2C protein phosphatase, thus inhibition of protein phosphatase activity blocks increase in PAL activity without affecting the increase in PAL protein levels
-
additional information
-
red light, acting via phytochrome, stimulates phenylalanine ammonia lyase activity in cotyledons and hypocotyls of tomato seedlings in a manner dependent on de novo synthesis of protein and nucleic acid. Photostimulation of PAL activity likely requires dephosphorylation by a type 2C protein phosphatase, thus inhibition of protein phosphatase activity blocks increase in PAL activity without affecting the increase in PAL protein levels
-
additional information
the enzyme expression is incuced by diverse factors, including pathogenic attack, tissue wounding and UV irradiation, and low temperature
-
additional information
-
PAL1 and PAL2 are upregulated 1.3-3.8fold in transgenic cells expressing recombinant plant oncogene rolB of Agrobacterium rhizogenes, overview
-
additional information
at low concentrations of indole butyric acid (0.0001 and 0.001 mM), there is no significant stimulatory effect on PAL specific activity
-
additional information
-
at low concentrations of indole butyric acid (0.0001 and 0.001 mM), there is no significant stimulatory effect on PAL specific activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.07
(2E)-3-(3-fluorophenyl)prop-2-enoic acid
pH 8.3, 30°C
3.3
(2E)-3-(3-hydroxyphenyl)prop-2-enoic acid
pH 8.3, 30°C
0.12
(2E)-3-(4-fluorophenyl)prop-2-enoic acid
pH 8.3, 30°C
0.66
(2E)-3-(4-nitrophenyl)prop-2-enoic acid
pH 8.3, 30°C
0.39
(2E)-3-(pyridin-3-yl)prop-2-enoic acid
pH 8.3, 30°C
0.38
(2E)-3-(pyridin-4-yl)prop-2-enoic acid
pH 8.3, 30°C
0.03
(2E)-3-phenylprop-2-enoic acid
pH 8.3, 30°C
1.51
(2E)-3-[4-(trifluoromethyl)phenyl]prop-2-enoic acid
pH 8.3, 30°C
0.3 - 0.7
(2E)-4-fluoro-cinnamic acid
0.1 - 0.4
(2E)-4-formyl-cinnamic acid
5.9 - 12.6
(2E)-4-hydroxycinnamate
0.1 - 0.5
(2E)-4-methyl-cinnamic acid
2.8 - 4.2
(2E)-4-nitro-cinnamic acid
0.75
(2S)-2-amino-3-(3-fluorophenyl)propanoic acid
pH 8.3, 30°C
1.11
(2S)-2-amino-3-(3-hydroxyphenyl)propanoic acid
pH 8.3, 30°C
0.56
(2S)-2-amino-3-(4-fluorophenyl)propanoic acid
pH 8.3, 30°C
0.23
(2S)-2-amino-3-(4-nitrophenyl)propanoic acid
pH 8.3, 30°C
3.39
(2S)-2-amino-3-(pyridin-3-yl)propanoic acid
pH 8.3, 30°C
0.48
(2S)-2-amino-3-(pyridin-4-yl)propanoic acid
pH 8.3, 30°C
0.29
(2S)-2-amino-3-phenylpropanoic acid
pH 8.3, 30°C
1.05
(2S)-2-amino-3-[4-(trifluoromethyl)phenyl]propanoic acid
pH 8.3, 30°C
0.076
2,3,4,5,6-pentafluoro-L-phenylalanine
-
-
0.085
2,6-difluoro-L-phenylalanine
-
-
0.048
2-amino-3-(1-benzofuran-2-yl)propanoic acid
-
pH 8.8, 30°C
0.116
2-amino-3-(1-benzothien-2-yl)propanoic acid
-
pH 8.8, 30°C
0.076
2-amino-3-(2-furyl)propanoic acid
-
pH 8.8, 30°C
0.134
2-amino-3-(2-thienyl)propanoic acid
-
pH 8.8, 30°C
0.018
2-amino-3-(3-thienyl)propanoic acid
-
pH 8.8, 30°C
0.05
2-chloro-L-phenylalanine
-
-
0.065
2-fluoro-L-phenylalanine
-
-
0.159
3,5-difluoro-L-phenylalanine
-
-
0.094
3-chloro-L-phenylalanine
-
-
0.079
3-fluoro-L-phenylalanine
-
-
0.045
4-chloro-L-phenylalanine
-
-
0.01 - 0.4
4-fluoro-L-phenylalanine
2 - 2.2
4-nitro-L-phenylalanine
2.5 - 3.1
4-trifluoromethyl-L-phenylalanine
0.022 - 42.4
L-phenylalanine
16
L-propargylglycine
-
pH 8.8, 30°C
0.186 - 4.384
L-styrylalanine
6.6
N-methyl-L-phenylalanine
-
-
0.05
phenylalanine
-
C503S/C565S mutant PAL
0.0783 - 0.154
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
0.201 - 0.395
rac-(E)-2-amino-5-phenylpent-4-enoic acid
additional information
L-phenylalanine
0.3
(2E)-4-fluoro-cinnamic acid
-
wild-type, pH 10, 30°C
0.7
(2E)-4-fluoro-cinnamic acid
-
mutant F137V, pH 10, 30°C
0.1
(2E)-4-formyl-cinnamic acid
-
mutant F137V, pH 10, 30°C
0.4
(2E)-4-formyl-cinnamic acid
-
wild-type, pH 10, 30°C
5.9
(2E)-4-hydroxycinnamate
-
mutant F137V, pH 10, 30°C
12.6
(2E)-4-hydroxycinnamate
-
wild-type, pH 10, 30°C
0.1
(2E)-4-methyl-cinnamic acid
-
mutant F137V, pH 10, 30°C
0.5
(2E)-4-methyl-cinnamic acid
-
wild-type, pH 10, 30°C
2.8
(2E)-4-nitro-cinnamic acid
-
wild-type, pH 10, 30°C
4.2
(2E)-4-nitro-cinnamic acid
-
mutant F137V, pH 10, 30°C
0.2
(E)-cinnamate
-
mutant F137V, pH 10, 30°C
0.2
(E)-cinnamate
-
wild-type, pH 10, 30°C
0.01
4-fluoro-L-phenylalanine
-
-
0.4
4-fluoro-L-phenylalanine
-
mutant F137V, pH 10, 30°C
0.4
4-fluoro-L-phenylalanine
-
wild-type, pH 10, 30°C
2
4-nitro-L-phenylalanine
-
wild-type, pH 10, 30°C
2.2
4-nitro-L-phenylalanine
-
mutant F137V, pH 10, 30°C
2.5
4-trifluoromethyl-L-phenylalanine
-
mutant F137V, pH 10, 30°C
3.1
4-trifluoromethyl-L-phenylalanine
-
wild-type, pH 10, 30°C
0.0065
L-Phe
-
at low substrate concentrations
0.011
L-Phe
-
at low substrate concentrations
0.011
L-Phe
-
two different Km-values: 0.011 mM and 0.055 mM
0.015
L-Phe
-
isoenzyme PAL-4
0.016
L-Phe
-
at high substrate concentrations
0.0169
L-Phe
-
isoenzyme PAL-2
0.0172
L-Phe
-
isoenzyme PAL-1
0.023
L-Phe
-
pH 8.0, 30°C, wild-type enzyme
0.0245
L-Phe
-
isoenzyme PAL-3
0.027
L-Phe
-
pH 8.8, 30°C, mutant enzyme Q487A
0.029
L-Phe
-
at low substrate substrate concentrations
0.03
L-Phe
-
tissue culture
0.032
L-Phe
-
at low concentrations
0.033
L-Phe
-
pH 8.8, 30°C, mutant enzyme Y350F
0.038
L-Phe
-
at low substrate concentrations
0.04
L-Phe
-
enzyme form 1
0.043
L-Phe
-
at low substrate concentrations
0.044
L-Phe
-
at low substrate concentrations
0.052
L-Phe
-
at low substrate concentrations
0.055
L-Phe
-
two different Km-values: 0.011 mM and 0.055 mM
0.07
L-Phe
-
enzyme form 2
0.078
L-Phe
-
at high substrate concentrations
0.091
L-Phe
-
at high substrate concentrations
0.11
L-Phe
-
enzyme form 3
0.12
L-Phe
-
pH 8.0, 30°C, mutant enzyme V83A
0.121
L-Phe
-
enzyme form PAL-II
0.16
L-Phe
Streptomyces verticillatus
-
-
0.18
L-Phe
-
at low substrate concentrations
0.23
L-Phe
wild-type, pH 8.5, 37°C
0.24
L-Phe
-
at high substrate concentrations
0.25
L-Phe
recombinant protein from Escherichia coli, pH 8.5, 37°C
0.26
L-Phe
-
at high substrate concentrations
0.27
L-Phe
-
at high substrate concentrations
0.29
L-Phe
-
at high substrate concentrations
0.331
L-Phe
recombinant protein from Pichia pastoris, pH 8.5, 37°C
0.333
L-Phe
wild-type, pH 8.5, 37°C
0.465
L-Phe
-
enzyme form PAL-III
0.8
L-Phe
-
at high substrate concentrationas
0.84
L-Phe
-
enzyme form PAL-I
2.288
L-Phe
mutant F134H, pH 8.5, 37°C
4.22
L-Phe
mutant F134H, pH 8.5, 37°C
5
L-Phe
-
at high substrate concentrations
14.2
L-Phe
-
pH 8.8, 30°C, mutant enzyme L137H
14.2
L-Phe
-
free enzyme, pH 8.7, 30°C
15
L-Phe
Rhodotorula texensis
-
-
64.9
L-Phe
-
immobilized enzyme, pH 8.7, 30°C
75.6
L-Phe
-
pH 8.8, 30°C, mutant enzyme L137H/Q487E
0.022
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme Q487A
0.028
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme Y350F
0.028
L-phenylalanine
-
enzyme from fruit ripened at low temperature, first Km value using low substrate concentrations, pH 8.8, 30°C
0.032
L-phenylalanine
-
pH 8.8, 30°C
0.033
L-phenylalanine
-
-
0.0364
L-phenylalanine
isoform PAL3, at 30°C in 50 mM Tris/HCl, pH 8.5
0.0395
L-phenylalanine
isoform PAL2, at 30°C in 50 mM Tris/HCl, pH 8.5
0.04
L-phenylalanine
-
enzyme from fruit ripened at room temperature, pH 8.8, 30°C
0.0428
L-phenylalanine
wild-type, pH 9.0, 37°C
0.045
L-phenylalanine
-
wild-type, pH 8.5, 37°C
0.049
L-phenylalanine
-
enzyme from fruit ripened in 20% CO2 atmosphere, first Km value using low substrate concentrations, pH 8.8, 30°C
0.05
L-phenylalanine
pH 8.8, 30°C
0.05
L-phenylalanine
pH 8.8, 30°C
0.0524
L-phenylalanine
isoform PAL4, at 30°C in 50 mM Tris/HCl, pH 8.5
0.0598
L-phenylalanine
isoform PAL1, at 30°C in 50 mM Tris/HCl, pH 8.5
0.06
L-phenylalanine
-
wild-type, pH 8.5, 37°C
0.06
L-phenylalanine
-
mutant lacking 21 N-terminal amino acids, pH 8.5, 37°C
0.06
L-phenylalanine
-
wild-type PAL
0.06
L-phenylalanine
wild-type, pH and temperature not specified in the publication
0.06 - 0.18
L-phenylalanine
-
enzyme from cultivar Verdial, in 37.5 mM borate buffer pH 8.8, at 40°C
0.069
L-phenylalanine
-
mutant L108A, pH 8.5, 37°C
0.07
L-phenylalanine
-
mutant L108G, pH 8.5, 37°C
0.077
L-phenylalanine
-
37°C, pH 7.5, wild-type enzyme
0.078
L-phenylalanine
-
37°C, pH 7.5, mutant enzyme E75L
0.08
L-phenylalanine
mutant Q292C/C565S, pH and temperature not specified in the publication
0.083
L-phenylalanine
-
pH 8.8, 30°C, wild-type enzyme
0.086
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme F137V
0.099
L-phenylalanine
-
37°C, pH 7.5, mutant enzyme E75A
0.101
L-phenylalanine
-
37°C, pH 7.5, mutant enzyme E75Q
0.112
L-phenylalanine
-
enzyme from fruit ripened in 20% CO2 atmosphere, second Km value using high substrate concentrations, pH 8.8, 30°C
0.112
L-phenylalanine
pH 8.5, 37°C, isozyme PAL3
0.12 - 0.25
L-phenylalanine
-
enzyme from cultivar Arbequina, in 37.5 mM borate buffer pH 8.8, at 40°C
0.13 - 0.32
L-phenylalanine
-
enzyme from cultivar Frantonio, in 37.5 mM borate buffer pH 8.8, at 40°C
0.144
L-phenylalanine
pH 8.5, 37°C, isozyme PAL2
0.152
L-phenylalanine
pH 8.5, 37°C, isozyme PAL1
0.164
L-phenylalanine
-
enzyme from fruit ripened at low temperature, second Km value using low substrate concentrations, pH 8.8, 30°C
0.18
L-phenylalanine
pH 8.5, 37°C, isozyme PAL4
0.23 - 0.3
L-phenylalanine
-
enzyme from cultivar Picual, in 37.5 mM borate buffer pH 8.8, at 40°C
0.25
L-phenylalanine
recombinant enzyme expressed in Escherichia coli
0.25
L-phenylalanine
recombinant enzyme expressed in Escherichia coli, at 37°C and pH 8.5
0.331
L-phenylalanine
recombinant enzyme expressed in Pichi pastoris
0.331
L-phenylalanine
recombinant enzyme expressed in Pichia pastoris, at 37°C and pH 8.5
0.5
L-phenylalanine
-
mutant F137V, pH 10, 30°C
0.52
L-phenylalanine
-
pH 8.8, 30°C
0.56
L-phenylalanine
-
pH 8.8, 30°C, soluble enzyme
0.6
L-phenylalanine
-
wild-type, pH 10, 30°C
1.01
L-phenylalanine
recombinant enzyme, in 50 mM Tris-HCl, pH 8.5, at 37°C
1.04
L-phenylalanine
-
pH 8.8, 30°C, encapsulated enzyme
1.33 - 1.75
L-phenylalanine
-
in presence or absence of D-phenylalanine
1.34
L-phenylalanine
-
pH 8, 40°C
1.386
L-phenylalanine
mutant F144H, pH 9.0, 37°C
1.5 - 2
L-phenylalanine
pH 8.0, 30°C, mutant enzyme
1.732
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme F137A
2.494
L-phenylalanine
pH 9.0, 55°C
4.2
L-phenylalanine
-
pH 8.5, 37°C, Vmax: 7.2 microM/min, trial 3
4.969
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme F137G
5
L-phenylalanine
-
pH 8.5, 37°C, Vmax: 1.3 microM/min, trial 1
5.7
L-phenylalanine
-
pH 8.5, 37°C, Vmax: 4.7 microM/min, trial 2
9.8
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme L137H
42.4
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme L137H/Q487E
0.186
L-styrylalanine
-
pH 8.8, 30°C, mutant enzyme F137V
1.173
L-styrylalanine
-
pH 8.8, 30°C, mutant enzyme F137A
4.12
L-styrylalanine
-
pH 8.8, 30°C, mutant enzyme F137G
4.384
L-styrylalanine
-
pH 8.8, 30°C, wild-type enzyme
0.097
L-Tyr
pH 8.5, 37°C
0.335
L-Tyr
mutant F134H, pH 8.5, 37°C
0.993
L-Tyr
wild-type, pH 8.5, 37°C
2.3
L-Tyr
-
isoenzyme PAL-2
2.5
L-Tyr
-
isoenzyme PAL-1
2.6
L-Tyr
-
isoenzyme PAL-4
7.8
L-Tyr
-
isoenzyme PAL-3
0.4
L-tyrosine
-
wild-type, pH 10, 30°C
0.532
L-tyrosine
mutant F144H, pH 9.0, 37°C
0.9
L-tyrosine
-
pH 8.5, 37°C, Vmax: 0.82 microM/min, trial 3
1.049
L-tyrosine
wild-type, pH 9.0, 37°C
1.68
L-tyrosine
pH 8.8, 30°C
2
L-tyrosine
-
pH 8.5, 37°C, Vmax: 1 microM/min, trial 2
2.4
L-tyrosine
-
pH 8.5, 37°C, Vmax: 0.2 microM/min, trial 1
2.6
NH3
-
pH 10.0
0.0783
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
0.154
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
0.201
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
0.395
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
0.05
trans-cinnamate
pH 10, 30°C
0.05
trans-cinnamate
pH 10, 30°C
additional information
L-phenylalanine
-
the Km-value of encapsulated enzyme in biomimetic silica is higher than that of the soluble enzyme due to lower total surface area and increased mass transfer resistance
additional information
additional information
-
influence of assay conditions on the Km-value
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
amination reaction kinetic parameters of wild-type PAM and mutants, all with an enantiomeric excess of over 99% (ee). Michaelis-Menten kinetics of formation of alpha- and beta-phenylalanine from trans-cinnamate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.08
(2E)-3-(3-fluorophenyl)prop-2-enoic acid
pH 8.3, 30°C
0.61
(2E)-3-(3-hydroxyphenyl)prop-2-enoic acid
pH 8.3, 30°C
0.09
(2E)-3-(4-fluorophenyl)prop-2-enoic acid
pH 8.3, 30°C
3.81
(2E)-3-(4-nitrophenyl)prop-2-enoic acid
pH 8.3, 30°C
0.14
(2E)-3-(pyridin-3-yl)prop-2-enoic acid
pH 8.3, 30°C
1.06
(2E)-3-(pyridin-4-yl)prop-2-enoic acid
pH 8.3, 30°C
2.22 - 6.7
(2E)-3-bromo-cinnamic acid
2.52 - 8.63
(2E)-3-fluoro-cinnamic acid
0.78 - 2.76
(2E)-3-nitro-cinnamic acid
0.03
(2E)-3-phenylprop-2-enoic acid
pH 8.3, 30°C
3.14
(2E)-3-[4-(trifluoromethyl)phenyl]prop-2-enoic acid
pH 8.3, 30°C
0.33 - 9.26
(2E)-4-bromo-cinnamic acid
2.14
(2E)-4-fluoro-cinnamic acid
pH 9.0, 30°C, wild-type enzyme
1.1
(2S)-2-amino-3-(3-fluorophenyl)propanoic acid
pH 8.3, 30°C
0.89
(2S)-2-amino-3-(3-hydroxyphenyl)propanoic acid
pH 8.3, 30°C
1.06
(2S)-2-amino-3-(4-fluorophenyl)propanoic acid
pH 8.3, 30°C
1.08
(2S)-2-amino-3-(4-nitrophenyl)propanoic acid
pH 8.3, 30°C
0.91
(2S)-2-amino-3-(pyridin-3-yl)propanoic acid
pH 8.3, 30°C
0.61
(2S)-2-amino-3-(pyridin-4-yl)propanoic acid
pH 8.3, 30°C
0.49
(2S)-2-amino-3-phenylpropanoic acid
pH 8.3, 30°C
0.82
(2S)-2-amino-3-[4-(trifluoromethyl)phenyl]propanoic acid
pH 8.3, 30°C
0.052 - 115.8
L-phenylalanine
0.37
L-propargylglycine
-
pH 8.8, 30°C
0.0345 - 0.422
L-styrylalanine
0.22
N-methyl-L-phenylalanine
-
-
4
phenylalanine
-
C503S/C565S mutant PAL
0.00024 - 0.0786
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
0.0062 - 0.276
rac-(E)-2-amino-5-phenylpent-4-enoic acid
0.39 - 3.46
trans-cinnamate
2.22
(2E)-3-bromo-cinnamic acid
pH 9.0, 30°C, wild-type enzyme
2.97
(2E)-3-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143C/Q144N
3.12
(2E)-3-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143S/Q144N
6.7
(2E)-3-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144C
2.52
(2E)-3-fluoro-cinnamic acid
pH 9.0, 30°C, wild-type enzyme
4.66
(2E)-3-fluoro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143S/Q144N
5.43
(2E)-3-fluoro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144C
6.7
(2E)-3-fluoro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144S
8.63
(2E)-3-fluoro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143C/Q144N
0.78
(2E)-3-nitro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144S
1.06
(2E)-3-nitro-cinnamic acid
pH 9.0, 30°C, wild-type enzyme
1.31
(2E)-3-nitro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143S/Q144N
2.71
(2E)-3-nitro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144C
2.76
(2E)-3-nitro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143C/Q144N
0.33
(2E)-4-bromo-cinnamic acid
pH 9.0, 30°C, wild-type enzyme
2.53
(2E)-4-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144S
4.83
(2E)-4-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143S/Q144N
5.99
(2E)-4-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144C
9.26
(2E)-4-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143C/Q144N
0.1
L-Phe
pH 8.8, 31°C
4.79
L-Phe
-
pH 8.0, 30°C, wild-type enzyme
7.8
L-Phe
mutant F134H, pH 8.5, 37°C
10.12
L-Phe
recombinant protein from Escherichia coli, pH 8.5, 37°C
16.04
L-Phe
recombinant protein from Pichia pastoris, pH 8.5, 37°C
16.3
L-Phe
wild-type, pH 8.5, 37°C
19.2
L-Phe
mutant F134H, pH 8.5, 37°C
21.3
L-Phe
wild-type, pH 8.5, 37°C
0.052
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme F137G
0.173
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme F137V
0.283
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme F137A
0.362
L-phenylalanine
pH 8.5, 37°C, isozyme PAL3
0.457
L-phenylalanine
pH 8.5, 37°C, isozyme PAL2
0.516
L-phenylalanine
pH 8.5, 37°C, isozyme PAL4
0.588
L-phenylalanine
pH 8.5, 37°C, isozyme PAL1
0.694
L-phenylalanine
-
pH 8.8, 30°C, wild-type enzyme
0.78
L-phenylalanine
isoform PAL3, at 30°C in 50 mM Tris/HCl, pH 8.5
0.95
L-phenylalanine
-
mutant L108G, pH 8.5, 37°C
1.09
L-phenylalanine
isoform PAL1, at 30°C in 50 mM Tris/HCl, pH 8.5
1.14
L-phenylalanine
isoform PAL2, at 30°C in 50 mM Tris/HCl, pH 8.5
1.53
L-phenylalanine
isoform PAL4, at 30°C in 50 mM Tris/HCl, pH 8.5
1.599
L-phenylalanine
-
37°C, pH 7.5, wild-type enzyme
1.84
L-phenylalanine
-
37°C, pH 7.5, mutant enzyme E75L
1.96
L-phenylalanine
-
wild-type, pH 8.5, 37°C
2.2
L-phenylalanine
pH 8.0, 30°C
2.28
L-phenylalanine
-
pH 8.8, 30°C
2.399
L-phenylalanine
-
37°C, pH 7.5, mutant enzyme E75A
2.478
L-phenylalanine
-
37°C, pH 7.5, mutant enzyme E75Q
2.6
L-phenylalanine
pH 8.8, 30°C
2.64
L-phenylalanine
pH 8.8, 30°C
3.6
L-phenylalanine
-
mutant L108A, pH 8.5, 37°C
3.9
L-phenylalanine
mutant Q292C/C565S, pH and temperature not specified in the publication
4.2
L-phenylalanine
wild-type, pH and temperature not specified in the publication
4.4
L-phenylalanine
-
wild-type, pH 8.5, 37°C
4.6
L-phenylalanine
-
mutant lacking 21 N-terminal amino acids, pH 8.5, 37°C
4.6
L-phenylalanine
-
wild-type PAL
10.11
L-phenylalanine
recombinant enzyme, in 50 mM Tris-HCl, pH 8.5, at 37°C
10.12
L-phenylalanine
recombinant enzyme expressed in Escherichia coli
10.12
L-phenylalanine
recombinant enzyme expressed in Escherichia coli, at 37°C and pH 8.5
16.04
L-phenylalanine
recombinant enzyme expressed in Pichi pastoris
16.04
L-phenylalanine
recombinant enzyme expressed in Pichia pastoris, at 37°C and pH 8.5
25.7
L-phenylalanine
-
pH 8, 40°C
47.3
L-phenylalanine
mutant F144H, pH 9.0, 37°C
65
L-phenylalanine
wild-type, pH 9.0, 37°C
115.8
L-phenylalanine
wild-type, pH 9.0, 37°C
0.0345
L-styrylalanine
-
pH 8.8, 30°C, mutant enzyme F137G
0.0471
L-styrylalanine
-
pH 8.8, 30°C, wild-type enzyme
0.132
L-styrylalanine
-
pH 8.8, 30°C, mutant enzyme F137A
0.422
L-styrylalanine
-
pH 8.8, 30°C, mutant enzyme F137V
0.03
L-Tyr
wild-type, pH 8.5, 37°C
0.1
L-Tyr
mutant F134H, pH 8.5, 37°C
0.05
L-tyrosine
pH 8.8, 30°C
0.084
L-tyrosine
wild-type, pH 9.0, 37°C
0.75
L-tyrosine
mutant F144H, pH 9.0, 37°C
0.00024
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
0.0786
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
0.0062
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
0.276
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
0.39
trans-cinnamate
pH 10, 30°C
0.46
trans-cinnamate
pH 10, 30°C
1.97
trans-cinnamate
pH 9.0, 30°C, wild-type enzyme
2.64
trans-cinnamate
pH 9.0, 30°C, mutant enzyme H143C/Q144N
3.46
trans-cinnamate
pH 9.0, 30°C, mutant enzyme H143N/Q144C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.89 - 5.04
(2E)-3-bromo-cinnamic acid
1.79 - 8.68
(2E)-3-fluoro-cinnamic acid
0.53 - 4.19
(2E)-3-nitro-cinnamic acid
0.22 - 29.38
(2E)-4-bromo-cinnamic acid
1.26
(2E)-4-fluoro-cinnamic acid
pH 9.0, 30°C, wild-type enzyme
1.47
(2S)-2-amino-3-(3-fluorophenyl)propanoic acid
pH 8.3, 30°C
0.8
(2S)-2-amino-3-(3-hydroxyphenyl)propanoic acid
pH 8.3, 30°C
1.89
(2S)-2-amino-3-(4-fluorophenyl)propanoic acid
pH 8.3, 30°C
4.7
(2S)-2-amino-3-(4-nitrophenyl)propanoic acid
pH 8.3, 30°C
0.27
(2S)-2-amino-3-(pyridin-3-yl)propanoic acid
pH 8.3, 30°C
1.27
(2S)-2-amino-3-(pyridin-4-yl)propanoic acid
pH 8.3, 30°C
1.69
(2S)-2-amino-3-phenylpropanoic acid
pH 8.3, 30°C
0.78
(2S)-2-amino-3-[4-(trifluoromethyl)phenyl]propanoic acid
pH 8.3, 30°C
0.81
3-chloro-L-phenylalanine
pH 8.8, 37°C
0.84
4-fluoro-L-phenylalanine
pH 8.8, 37°C
0.0104 - 19200
L-phenylalanine
0.0083 - 2.269
L-styrylalanine
0.03
L-tyrosine
pH 8.8, 30°C
0.0015 - 1.004
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
0.0156 - 1.373
rac-(E)-2-amino-5-phenylpent-4-enoic acid
1.27 - 9.13
trans-cinnamate
0.89
(2E)-3-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143S/Q144N
2.72
(2E)-3-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143C/Q144N
3.45
(2E)-3-bromo-cinnamic acid
pH 9.0, 30°C, wild-type enzyme
5.04
(2E)-3-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144C
1.79
(2E)-3-fluoro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144S
2.81
(2E)-3-fluoro-cinnamic acid
pH 9.0, 30°C, wild-type enzyme
3.38
(2E)-3-fluoro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143S/Q144N
4.29
(2E)-3-fluoro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144C
8.68
(2E)-3-fluoro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143C/Q144N
0.53
(2E)-3-nitro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144S
0.55
(2E)-3-nitro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143S/Q144N
1.24
(2E)-3-nitro-cinnamic acid
pH 9.0, 30°C, wild-type enzyme
2.17
(2E)-3-nitro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144C
4.19
(2E)-3-nitro-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143C/Q144N
0.22
(2E)-4-bromo-cinnamic acid
pH 9.0, 30°C, wild-type enzyme
5.76
(2E)-4-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144S
7.2
(2E)-4-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143S/Q144N
14.97
(2E)-4-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143C/Q144N
29.38
(2E)-4-bromo-cinnamic acid
pH 9.0, 30°C, mutant enzyme H143N/Q144C
0.18
L-Phe
mutant F134H, pH 8.5, 37°C
8.4
L-Phe
mutant F134H, pH 8.5, 37°C
40.5
L-Phe
recombinant protein from Escherichia coli, pH 8.5, 37°C
48.5
L-Phe
recombinant protein from Pichia pastoris, pH 8.5, 37°C
63.9
L-Phe
wild-type, pH 8.5, 37°C
70.8
L-Phe
wild-type, pH 8.5, 37°C
0.0104
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme F137G
0.163
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme F137A
0.51
L-phenylalanine
pH 8.8, 37°C
1.45
L-phenylalanine
pH 8.0, 30°C, mutant enzyme
2.011
L-phenylalanine
-
pH 8.8, 30°C, mutant enzyme F137V
4.05
L-phenylalanine
recombinant enzyme expressed in Escherichia coli
4.85
L-phenylalanine
recombinant enzyme expressed in Pichi pastoris
8.361
L-phenylalanine
-
pH 8.8, 30°C, wild-type enzyme
10
L-phenylalanine
recombinant enzyme, in 50 mM Tris-HCl, pH 8.5, at 37°C
18.28
L-phenylalanine
isoform PAL1, at 30°C in 50 mM Tris/HCl, pH 8.5
20.77
L-phenylalanine
-
37°C, pH 7.5, wild-type enzyme
21.1
L-phenylalanine
isoform PAL3, at 30°C in 50 mM Tris/HCl, pH 8.5
23.58
L-phenylalanine
-
37°C, pH 7.5, mutant enzyme E75L
24.26
L-phenylalanine
-
37°C, pH 7.5, mutant enzyme E75A
24.46
L-phenylalanine
-
37°C, pH 7.5, mutant enzyme E75Q
28.93
L-phenylalanine
isoform PAL2, at 30°C in 50 mM Tris/HCl, pH 8.5
29.09
L-phenylalanine
isoform PAL4, at 30°C in 50 mM Tris/HCl, pH 8.5
49
L-phenylalanine
mutant Q292C/C565S, pH and temperature not specified in the publication
55.06
L-phenylalanine
pH 8.8, 30°C
56.62
L-phenylalanine
pH 8.8, 30°C
70
L-phenylalanine
wild-type, pH and temperature not specified in the publication
19200
L-phenylalanine
-
pH 8, 40°C
0.0083
L-styrylalanine
-
pH 8.8, 30°C, mutant enzyme F137G
0.0107
L-styrylalanine
-
pH 8.8, 30°C, wild-type enzyme
0.1125
L-styrylalanine
-
pH 8.8, 30°C, mutant enzyme F137A
2.269
L-styrylalanine
-
pH 8.8, 30°C, mutant enzyme F137V
0.028
L-Tyr
wild-type, pH 8.5, 37°C
0.31
L-Tyr
mutant F134H, pH 8.5, 37°C
0.0015
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
1.004
rac-(E)-2-amino-5-(4-chlorophenyl)pent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
0.0156
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, wild-type enzyme
1.373
rac-(E)-2-amino-5-phenylpent-4-enoic acid
-
pH 8.8, 30°C, mutant enzyme F137V
1.27
trans-cinnamate
pH 9.0, 30°C, mutant enzyme H143N/Q144C
1.55
trans-cinnamate
pH 9.0, 30°C, mutant enzyme H143C/Q144N
2.75
trans-cinnamate
pH 9.0, 30°C, wild-type enzyme
8.19
trans-cinnamate
pH 10, 30°C
9.13
trans-cinnamate
pH 10, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-
in Penicillium digitatum non-infected areas, the actvities of superoxide dismutase, EC 1.15.1.1, catalase, EC 1.11.1.6, ascorbate peroxidase, EC 1.11.1.11, and glutathione reductase, EC 1.6.4.2, as well as soluble and insoluble peroxidase, EC 1.11.1.7, and phenylalanine ammonia-lyase, EC 4.3.1.24 are higher in flavedo than in alvedo
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
vascular tissue, AtPAL1 and AtPAL2
brenda
-
brenda
-
brenda
-
brenda
-
-
brenda
-
brenda
-
brenda
-
-
brenda
AtPAL1 and AtPAL2
brenda
-
-
brenda
-
-
-
brenda
high expression, expression levels increase in the order green leaves, turning color leaves, bracts. Diurnal variation of PAL expression level in bracts exhibits two highest peaks at 9:00 and 18:00, respectively, and reaches the lowest level at 12:00 in a clear day
brenda
-
high expression, expression levels increase in the order green leaves, turning color leaves, bracts. Diurnal variation of PAL expression level in bracts exhibits two highest peaks at 9:00 and 18:00, respectively, and reaches the lowest level at 12:00 in a clear day
-
brenda
low expression
brenda
high transcript level
brenda
level of enzyme mRNA increases 5 days after the establishment of in vitro callus unions. Enzyme transcription shows a higher level in graft union of incompatible partners and does not result in formation of lignin
brenda
level of enzyme mRNA increases 5 days after the establishment of in vitro callus unions. Enzyme transcription shows a higher level in graft union of incompatible partners and does not result in formation of lignin
brenda
-
brenda
-
VB2 and VB1 callus cultures
brenda
-
-
brenda
-
-
brenda
-
kinetin-treated and untreated cells
brenda
-
-
brenda
-
-
brenda
-
brenda
DcPAL3 gene expression occurs in anthocyanin-synthesizing cells
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
from seddlings, 74 kDa isozyme
brenda
-
-
brenda
-
in Penicillium digitatum non-infected areas, the actvities of superoxide dismutase, EC 1.15.1.1, catalase, EC 1.11.1.6, ascorbate peroxidase, EC 1.11.1.11, and glutathione reductase, EC 1.6.4.2, as well as soluble and insoluble peroxidase, EC 1.11.1.7, and phenylalanine ammonia-lyase, EC 4.3.1.24 are higher in flavedo than in alvedo. Upon infection, phenylalanine ammonia-lyase activity and transcript level in flavedo increases, but Penicillium digitatum can suppress this defencse response
brenda
highest expression
brenda
transcript levels are higher in bud flowers and wilting flowers than in blooming flowers
brenda
the transcriptional level of LrPAL3 is positively associated with the galanthamine contents within the leaves and flowers, which suggested that the expression and function is coregulated and involved in the biosynthesis of galanthamine
brenda
-
transcripts of RiPAL1 and RiPAL2
brenda
highest expression of PAL1 in roots, followed by leaves, stems and flowers
brenda
PAL3 has the highest expression in leaves, less in roots, stems and flowers
brenda
SmPAL2 was predominately expressed in stems and flowers
brenda
MG745168
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
expression of isoform PAL6 is fruit-specific, and increases during fruit ripening in both cultivars along with anthocyanin accumulation. PAL enzyme activity increases at similar rates in both cultivars at early ripening stages, but at the end of ripening PAL activity diminishes in cultivar Toyonoka while it rises markedly in cultivar Camarosa. PAL activity is higher in internal fruit tissue, showing no correlation with anthocyanin level of the same section in both cultivars. The higher FaPAL6 expression and activity detected in Camarosa may be associated to the enhanced anthocyanin accumulation found in this cultivar
brenda
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-
brenda
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-
brenda
-
brenda
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-
brenda
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-
brenda
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-
brenda
-
transcripts of RiPAL1 and RiPAL2
brenda
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-
brenda
berry
brenda
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-
brenda
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-
brenda
-
induced by a Verticillium dahliae phytotoxin
brenda
-
brenda
vascular tissue, AtPAL1 and AtPAL2
brenda
-
brenda
PAL expression is constitutive in leaves throughout development and decline only in the most mature stage, overview
brenda
-
-
brenda
-
-
brenda
-
-
brenda
low expression, expression levels increase in the order green leaves, turning color leaves, bracts
brenda
-
low expression, expression levels increase in the order green leaves, turning color leaves, bracts
-
brenda
-
-
brenda
high expression level
brenda
expression in all tissues tested, most highly in flowers, followed by stem and leaf, and lowest in root and seed
brenda
-
-
brenda
-
transcripts for the wound-inducible enzyme LsPAL1 accumulate in cells close to the wound sites. PAL mRNA is associated with tissue next to the epidermis and vascular bundles
brenda
the transcriptional level of LrPAL3 is positively associated with the galanthamine contents within the leaves and flowers, which suggested that the expression and function is coregulated and involved in the biosynthesis of galanthamine
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
very low levels of RiPAL transcripts
brenda
highest expression of PAL1 in roots, followed by leaves, stems and flowers
brenda
PAL3 has the highest expression in leaves, less in roots, stems and flowers
brenda
-
-
brenda
-
brenda
-
-
brenda
from seedlings, three isozymes of 74 kDa, 83 kDa, and 103 kDa molecular weight
brenda
MG745168
-
brenda
-
-
-
brenda
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sheath tissue of shoots
brenda
-
2 different enzyme forms are isolated after 68 h and after 116 h: PAL68 and PAL116
brenda
-
-
brenda
-
NRRL Y5484
brenda
higest expression
brenda
highly expressed in fine roots
brenda
vascular tissue, AtPAL1 and AtPAL2
brenda
-
brenda
-
brenda
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uncut and shredded carrots. Enzyme activity is induced by processing and linearly increased throughout storage under aerobic conditions. An anaerobic atmosphere results in a maximum activity peak at storage day 2-4. The use of chlorinated water for washing shredded carrots slightly delays the onset of PAL activity
brenda
-
brenda
high expression
brenda
-
high expression
-
brenda
-
-
brenda
-
-
brenda
expression in all tissues tested, most highly in flowers, followed by stem and leaf, and lowest in root and seed
brenda
low transcript level
brenda
-
-
brenda
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cultured Morinda citrifolia adventitious roots in different strength, i.e. 0.25, 0.50, 0.75, 1.0, 1.5 and 2.0 of Murashige and Skoog medium supplemented with 5 mg/l indole butyric acid and 30 g/l sucrose
brenda
-
brenda
low expression level
brenda
-
transcripts of RiPAL1 and RiPAL2
brenda
highest expression of PAL1 in roots, followed by leaves, stems and flowers
brenda
PAL3 has the highest expression in leaves, less in roots, stems and flowers
brenda
-
-
brenda
from seedlings, 74 kDa isozyme
brenda
MG745168
-
brenda
-
-
-
brenda
the root tissues of the corn variety Japanese Striped corn contain greater levels of PAL gene transcripts and PAL activities, compared to those of the shoot tissues
brenda
-
enzyme activity changes during seed maturation and decreases steadily for up to 15 weeks after flowering from 336 to 211 U per g fresh weight, inverse relationship between enzyme protein content and activity
brenda
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-
brenda
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brenda
expression in all tissues tested, most highly in flowers, followed by stem and leaf, and lowest in root and seed
brenda
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-
brenda
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-
brenda
AtPAL1 and AtPAL2
brenda
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with four expanded leaves
brenda
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-
brenda
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PAL activity is greatly induced by mechanical wounding and aphid infestation in cotton seedlings. The iduction of PAL occurs not only in wounded and infested seedlings but also in intact healthy seddlings growing nearby
brenda
-
PAL activity is greatly induced by mechanical wounding and aphid infestation in cotton seedlings. The iduction of PAL occurs not only in wounded and infested seedlings but also in intact healthy seddlings growing nearby
-
brenda
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brenda
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brenda
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-
brenda
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-
brenda
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brenda
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-
brenda
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brenda
7-days-old
brenda
the PAL activity of young seedlings of the corn variety Indian Blue corn is generally 30-50% lower than those of cultivar Japanese Striped corn seedlings at equivalent growth stages
brenda
-
brenda
-
brenda
in shoot and branch shoot, mainly localized to sclerenchymal cells
brenda
in shoot and branch shoot, mainly loclaized to sclerenchymal cells
brenda
-
transcripts of RiPAL1 and RiPAL2
brenda
-
-
brenda
the shoot tissues of the corn variety Japanese Striped corn contain lower levels of PAL gene transcripts and PAL activities, compared to those of the root tissues
brenda
-
-
brenda
low expression
brenda
-
low expression
-
brenda
high expression level
brenda
expression in all tissues tested, most highly in flowers, followed by stem and leaf, and lowest in root and seed
brenda
-
brenda
-
-
brenda
-
brenda
highest expression of PAL1 in roots, followed by leaves, stems and flowers
brenda
PAL3 has the highest expression in leaves, less in roots, stems and flowers
brenda
SmPAL2 was predominately expressed in stems and flowers
brenda
-
-
brenda
-
brenda
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diffenrentiating secondary xylem
brenda
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differentating
brenda
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xylem ray parenchymal cells
brenda
additional information
the expression of pal genes in the roots is higher than in the plants aerial parts, the activity of PAL in the roots is also higher than in the aerial parts
brenda
additional information
-
the expression of pal genes in the roots is higher than in the plants aerial parts, the activity of PAL in the roots is also higher than in the aerial parts
brenda
additional information
broad and constitutive tissue expression, temporal expression profiling analysis, overview
brenda
additional information
dry seeds of both varieties have no PAL activity
brenda
additional information
-
dry seeds of both varieties have no PAL activity
brenda
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malfunction
the pal1 pal2 double knockout mutant is almost devoid of flavonoids
metabolism
L-phenylalanine ammonia-lyase is the first enzyme of phenylpropanoid biosynthesis
metabolism
-
PAL is a major marker of phenylpropanoid pathway
metabolism
key enzymes in the phenylpropanoid pathway for the synthesis of flavones
metabolism
-
the enzyme is involved in the capsaicinoid biosynthesis pathway. For both control and drought-stressed plants, the activities differed significantly among cultivars. Enzyme activity is significantly increased for all of the cultivars under drought stress. Changes under drought stress show a complete association with capsaicinoids, in all cultivars
metabolism
AtPAL isogenes differentially respond to environmental stresses and AtPAL1 and AtPAL2 have functional specialization in environmentally triggered phenolic synthesis
metabolism
MG745168
enzyme of the phenylpropanoid pathway
metabolism
enzyme of the phenylpropanoid pathway
metabolism
-
enzyme of the plant phenylpropanoid pathway
metabolism
isogenes AtPAL1, 2, and 4 show close association with lignin biosynthesis
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
Streptomyces verticillatus
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
-
key gateway enzyme linking the phenylpropanoid secondary pathway to primary metabolism
metabolism
-
rate-limiting enzyme of phenolic biosynthetic pathway
metabolism
rate-limiting enzyme of phenolic biosynthetic pathway
metabolism
the enzyme has crucial role in secondary phenylpropanoid metabolism of plants
metabolism
the enzyme is involved in phenylpropanoid biosynthesis. The gateway enzyme plays a key role in mediating carbon flux from primary metabolism into the phenylpropanoid pathway
metabolism
the enzyme is involved in the biosynthesis of galanthamine, a Amaryllidaceae alkaloid, that is a clinically used drug for the treatment of Alzheimer's disease
metabolism
Coleus scutellarioides
the enzyme is involved in the phenylpropanoid pathway and plays important roles in the secondary metabolisms, development and defense of plants
metabolism
rain shelter treatment may affect phenylalanine lignin monomer synthesis and subsequent cork accumulation by altering the expression or enzyme activities of phenylalanine ammonia lyase (PAL), catechol-O-methyltransferase (COMT), cinnamoyl-CoA reductase (CCR), cinnamyl alcohol dehydrogenase (CAD), peroxidase (POD), and omega-hydroxypalmitate O-feruloyl transferase (HHT1), thus decreasing exocarp russet accumulation in semi-russet pear
metabolism
-
rate-limiting enzyme of phenolic biosynthetic pathway
-
metabolism
-
enzyme of the phenylpropanoid pathway
-
physiological function
-
activities of polyphenol oxidase and PAL are highest after cultivation at low day/night temperatures of 20/13°C, as is anthocyanin content
physiological function
-
during culture of Morinda citrifolia adventitious roots in different strength, i.e. 0.25, 0.50, 0.75, 1.0, 1.5 and 2.0 of Murashige and Skoog medium supplemented with 5 mg/l indole butyric acid and 30 g/l sucrose, phenylalanine ammonia lyase activity shows a positive correlation in relation to salt strength that leads to an increase in phenol biosynthesis in expense of anthraquinone formation. With the increasing salt strength, root growth and anthraquinone accumulation decrease significantly
physiological function
-
PAL activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 24 hours after inoculation in the resistant varieties. Defense enzymes PAL, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. PAL is induced first, followed by tyrosine ammonia-lyase and than polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
physiological function
-
suppression of PAL by RNAi leads to plants exhibiting phenotypes such as stunted growth, delayed root formation, altered leaves, and reduced lignin deposition. The total phenolic content is decreased by 20-70% in PAL-suppressed lines, and is accompanied by lower PAL activity. Down-regulation of PAL also affects the expression of cinnamate 4-hydroxylase, 4-coumarate:coenzyme A ligase2, and tyrosine aminotransferase, related genes in the rosmarinic acid pathway. Rosmarinic acid and salvianolic acid B are markedly reduced in PAL-suppressed lines
physiological function
Arabidopsis KFB proteins physically interact with and mediate the proteolytic turnover of four PAL isozymes (PAL1, PAL2, PAL3, PAL4)
physiological function
-
increases in PAL and CW-PRX activities are cooperatively involved in the formation of ferulate network in cell walls of rice shoots
physiological function
-
PAL activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 24 hours after inoculation in the resistant varieties. Defense enzymes PAL, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. PAL is induced first, followed by tyrosine ammonia-lyase and than polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
-
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F133H
decrease in ration kcat/KM value
F134H
decrease in ratio kcat/KM value
L108A
-
slight decrease in catalytic activity
L108G
-
slight decrease in catalytic activity
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%)
F137I
-
increased activity in the amination of p-nitro-cinnamic acid
F137T
-
increased activity in the amination of p-nitro-cinnamic acid
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
S202A
-
mutation results in lack of catalytic activity
Y350F
-
kinetic D isotope effect is of the same magnitude as wild-type enzyme
S153A
-
mutant shows no activity
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
-
site-directed mutagenesis
C565S
-
site-directed mutagenesis
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
L108A
-
slight decrease in catalytic activity
L108G
-
slight decrease in catalytic activity
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
-
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
-
F144H
decrease of activity with L-phenylalanine, increase of activity with L-tyrosine
F144H
-
marked reduction (30fold) in affinity for the substrate phenylalanine
F137V
-
increased activity in the amination of p-nitro-cinnamic acid
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
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C- or N-terminal His-tagged enzymes are expressed in Escherichia coli Rosetta 2 (DE3) cells
cloned into expression plasmid pHIS8. The recombinant EncP is overexpressed as an N-terminal octahistidyl-tagged fusion protein in Escherichia coli BL21
-
DNA and amino acid sequence determination and analysis, primers designed from GenBank sequence D26596, UniProt ID P45726, semiquantitative expression analysis by RT-PCR
DNA and amino acid sequence determination, analysis, and comparison of PAL isozymes, expression and phylogenetic analysis
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21 (DE3)
expressed in Nicotiana tabacum
expressed in Pichia pastoris strain X-33
expressed in Pichia pastoris strain X-33 and Escherichia coli Top10 cells
expression in Escherichia coli
expression in Escherichia coli an Pichia pastoris
expression in Escherichia coli and Pichia pastoris
expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli or Saccharomyces cerevisiae
expression in Escherichia coli strain JM109
expression in Streptomyces lividans
-
fusion proteins with gluthatione S-transferase expressed in Escherichia coli
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gene GbPAL, DNA and amino acid sequence determination and analysis, the gene is intron-less and belongs to a small multi-gene family, expression analysis and sequence comparison
gene pal1, genomic library screening, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, recombinant expression in Escherichia coli strain XL1-Blue, identification of cis-acting regulatory DNA elements
gene pal1, transcription profile, expression in Escherichia coli strain M15
gene pal2, genomic library screening, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, recombinant expression in Escherichia coli strain XL1-Blue, identification of cis-acting regulatory DNA elements
gene pal3a, genomic library screening, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, recombinant expression in Escherichia coli strain XL1-Blue, identification of cis-acting regulatory DNA elements
gene pal3b, genomic library screening, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, recombinant expression in Escherichia coli strain XL1-Blue, identification of cis-acting regulatory DNA elements
gene pal4, genomic library screening, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis, recombinant expression in Escherichia coli strain XL1-Blue, identification of cis-acting regulatory DNA elements
gene PALrs1, DNA and amino acid sequence determination and analysis, and analysis of egenomic structure, overview. Expression of PALrs1 under the 35S promoter with double-enhancer sequences from CaMV-W and TMV-W fragments in Rhodiola sachalinensis via Agrobacterium tumefaciens transfection method
overexpression in Coleus blumei
overexpression in Escherichia coli
PAL genes, multi-gene family with about 26 copies in the diploid genome, DNA and amino acid sequence determination and analysis, distribution of PAL gene sequences in the tomato genome, overview, very active silencing suggesting aggressive competition between PAL gene duplication and copy inactivation during PAL gene evolution, expression analysis of isozymes in plants, overview. Expression in Escherichia coli strain DH5alpha
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
the expression of genes PAL1 and PAL2, but not PAL3, is upregulated in transgenic cells expressing recombinant plant oncogene rolB of Agrobacterium rhizogenes, expression analysis, overview
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transient expression of a loss-of-function mutant DcPAL3 promoter-reporter construct in protoplasts prepared from carrot suspension-cultured cells, both the GCC-box homolog and the box-L are required for overall DcPAL3 expression. Possible different mechanism in the normal and variant cultured cell lines, respectively, in terms DcPAL3 promoter regulation
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expressed in Escherichia coli
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expressed in Escherichia coli
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expressed in Escherichia coli
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expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli as a His-tagged fusion protein
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
Coleus scutellarioides
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli BL21 (DE3)
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expression in Escherichia coli BL21 (DE3)
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expression in Escherichia coli BL21 (DE3)
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expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21 (DE3)
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0.25 mM salicylic acid sharply increases phenylalanine ammonia-lyase activity (24 h after application)
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a 4fold increase of PAL activity is observed in chitosan-stimulated cell cultures (0.01 mg/ml) at 24 h post-elicitation
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a gradual decrease in both phenylalanine ammonia lyase and tyrosine ammonia lyase activities are observed following infection of rhizomes of Zingiber officinale with Pythium myriotylum. This is in contrast to the gradual increase in phenylalanine ammonia lyase and tyrosine ammonia lyase specific activity after 5 days post infection in the wild taxon Zingiber zerumbet
activities of polyphenol oxidase and PAL are highest after cultivation at low day/night temperatures of 20/13°C, as is anthocyanin content
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downregulated by dark treatment
expression is induced by treatment with abscisic acid, gibberellin GA3, high and low temperature
expression of PAL transcripts peak 4 h after exposure to 0.05 mg/ml yeast elicitor, whereas 0.025 mM methyl jasmonate induction of PAL transcripts is slower
From 5 days post-anthesis to the onset of ripening PAL5 expression decreases gradually. PAL5 transcript level decreases after abscisic acid treatment (0.1 mM). Treatment with 10 mM H2O2 causes the PAL5 transcript level to decrease after 3 h, a similar decrease is observed for the PAL5 transcript after exposure to 0.05 mM methyl viologen for 3 h
highest expression level is present in the in vitro raised leaf and root samples as compared to that of the ex vitro plant
in response to 200 mM NaCl and 200 mM mannitol treatment the PAL5 transcript increases significantly after 1 h of treatment and begins to decline gradually from then on
in riboflavin-treated inoculated plants, upregulation of PAL expression is detected downstream of lipoxygenase upregulation
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increase in phenyl alanine ammonia lyase activity is observed at both the treatments of supplemental UV-B (pre-treatment of Psoralens against supplemental UV-B and supplemental UV-B) with maximum increment of 42.9% at pre-treatment of Psoralens against supplemental UV-B followed by 14.8% in supplemental UV-B as compared to the control at 20 days after germination
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induced by mechanical wounding
induced most strongly in response to 300 microM methyl jasmonate treatment at 6 h
isogenes AtPAL-1, -2, and -4 have much higher expression levels than AtPAL-3
methyl jasmonate treatment during storage significantly inhibits the increase in activity of PAL
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mRNA level of isoform PAL6 is higher in cultivar Camarosa than in cultivar Toyonoka
Muktakeshi cultivar shows a higher increase in the PAL activity with the concentrations of the 0.0012 mg/l eliciting solution in the cell suspension culture medium
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nitrogen depletion induces the expression of PAL1 and PAL2
PAL activity increases after 48 h of incubation with ethephon at 22°C and during fruit ripening
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PAL activity increases in both the leaf rosettes and the roots of Ni-treated chamomile (0.003-0.12 mM for 10 days)
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PAL activity of the 20-day-old immobilized Taxus cuspidata cells increases by 11% after 4 h treatment with 0.02 mM sodium nitroprusside
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PAL mRNA level is higher in seedlings growing in the presence of Pb2+ than in the control. The increase in activity is not directly correlated with the increase in mRNA
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PAL mRNA level is higher in soybean roots growing in the presence of Cd2+ or Pb2+ than in the control. The highest amount of mRNA coding for PAL is observed in the presence of 15 mg/l of Cd2+ or 50 mg/l of Pb2+. The increase in activity is not directly correlated with the increase in mRNA
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PAL mRNA level is lower in seedlings growing in the presence of Cd2+ than in the control
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pretreatment of mycelia with 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide or aminoguanidine suppresses PAL activity
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significantly down-regulated in the rain shelter group compared to those in the control group
SsPAL1 was constitutively expressed and is enhanced by light and different abiotic factors
Coleus scutellarioides
the activity of phenylalanine ammonia-lyase decreases in all treatments on the fifth day after inoculation of nematode over control. The reduction is significant in all the treatments except salicylic acid treatment
the expression of phenylalanine ammonia-lyase mRNA increases during cold storage of mung bean sprout. The increase in expression is inhibited by the heat-shock treatment of mung bean sprout before storage
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the second day following inoculation of nematode Pratylenchus thornei, the activity of phenylalanine ammonia-lyase increases significantly compared to control in all treatments. All seedlings treated by both inducers, salicylic acid and methyl jasmonate, show further increase over infected seedlings without inducer. Increasing is significant only in the nematode treatments free of salicylic acid
transcript levels in leaves are significantly induced by methyl jasmonate, nitric oxide, and salicylic acid
treatment of seedlings with 5 mM 3-aminobenzamide significantly reduces PAL activity in elf18-elicited seedlings
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upregulated by different types of abiotic stresses like wounding, cold, UV-B and salinity
a gradual decrease in both phenylalanine ammonia lyase and tyrosine ammonia lyase activities are observed following infection of rhizomes of Zingiber officinale with Pythium myriotylum. This is in contrast to the gradual increase in phenylalanine ammonia lyase and tyrosine ammonia lyase specific activity after 5 days post infection in the wild taxon Zingiber zerumbet
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a gradual decrease in both phenylalanine ammonia lyase and tyrosine ammonia lyase activities are observed following infection of rhizomes of Zingiber officinale with Pythium myriotylum. This is in contrast to the gradual increase in phenylalanine ammonia lyase and tyrosine ammonia lyase specific activity after 5 days post infection in the wild taxon Zingiber zerumbet
a gradual decrease in both phenylalanine ammonia lyase and tyrosine ammonia lyase activities are observed following infection of rhizomes of Zingiber officinale with Pythium myriotylum. This is in contrast to the gradual increase in phenylalanine ammonia lyase and tyrosine ammonia lyase specific activity after 5 days post infection in the wild taxon Zingiber zerumbet
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downregulated by dark treatment
MG745168
downregulated by dark treatment
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highest expression level is present in the in vitro raised leaf and root samples as compared to that of the ex vitro plant
MG745168
highest expression level is present in the in vitro raised leaf and root samples as compared to that of the ex vitro plant
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upregulated by different types of abiotic stresses like wounding, cold, UV-B and salinity
MG745168
upregulated by different types of abiotic stresses like wounding, cold, UV-B and salinity
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nutrition
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the enzyme can be used for the development of dietary foods and biotechnological products for patients with phenylketonuria
agriculture
level of enzyme mRNA increases 5 days after the establishment of in vitro callus unions. Enzyme transcription shows a higher level in graft union of incompatible partners and does not result in formation of lignin
agriculture
level of enzyme mRNA increases 5 days after the establishment of in vitro callus unions. Enzyme transcription shows a higher level in graft union of incompatible partners and does not result in formation of lignin
agriculture
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treatment of plants with Pseudmonas sp. increases shoot length and significantly increases the activity of both peroxidase and phenylalanine ammonia-lyase. Treatment may help plants against pathogen invasion by modulating plant peroxidase and phenylalanine ammonia-lyase activities
agriculture
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treatment of plants with Pseudmonas sp. increases shoot length and significantly increases the activity of both peroxidase and phenylalanine ammonia-lyase. Treatment may help plants against pathogen invasion by modulating plant peroxidase and phenylalanine ammonia-lyase activities
agriculture
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treatment of plants with Pseudomonas fluorescens and Pseudomonas aeruginosa induces enzyme synthesis associated with increased synthesis of phenolic compounds such as tannic, gallic, caffeic, chlorogenic and cinnamic acids. Treatment with Sclerotinia slerotiorum does not induce enzyme synthesis
agriculture
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during culture of Morinda citrifolia adventitious roots in different strength, i.e. 0.25, 0.50, 0.75, 1.0, 1.5 and 2.0 of Murashige and Skoog medium supplemented with 5 mg/l indole butyric acid and 30 g/l sucrose, phenylalanine ammonia lyase activity shows a positive correlation in relation to salt strength that leads to an increase in phenol biosynthesis in expense of anthraquinone formation. With the increasing salt strength, root growth and anthraquinone accumulation decrease significantly
agriculture
expression of isoform PAL6 is fruit-specific, and increases during fruit ripening in both cultivars along with anthocyanin accumulation. PAL enzyme activity increases at similar rates in both cultivars at early ripening stages, but at the end of ripening PAL activity diminishes in cultivar Toyonoka while it rises markedly in cultivar Camarosa. PAL activity is higher in internal fruit tissue, showing no correlation with anthocyanin level of the same section in both cultivars. The higher FaPAL6 expression and activity detected in Camarosa may be associated to the enhanced anthocyanin accumulation found in this cultivar
agriculture
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PAL activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 24 hours after inoculation in the resistant varieties. Defense enzymes PAL, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. PAL is induced first, followed by tyrosine ammonia-lyase and than polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
agriculture
transgenic roots of Coleus blumei, harbouring the Arabidopsis thaliana PAL1 gene, under the control of the CaMV 35S promoter, show disparate phenylalanine ammonia-lyase activities ranging from 67 to 350%, compared to wild-type roots. Growth rates significantly differ, with the lowest in transgenic roots exerting augmented phenylalanine ammonia-lyase activity. Transgenic roots with high phenylalanine ammonia-lyase activity have lower growth rates, lower amounts of total phenolics, rosmarinic acid, i.e. the major phenolic compound in Coleus blumei and chlorogenic acid, but increased amounts of caffeic acid. There is no increase in total phenolics and rosmarinic acid content after feeding transgenic roots with casein enzymatic hydrolysate and L-tyrosine
agriculture
rain shelter treatment may affect phenylalanine lignin monomer synthesis and subsequent cork accumulation by altering the expression or enzyme activities of phenylalanine ammonia lyase (PAL), catechol-O-methyltransferase (COMT), cinnamoyl-CoA reductase (CCR), cinnamyl alcohol dehydrogenase (CAD), peroxidase (POD), and omega-hydroxypalmitate O-feruloyl transferase (HHT1), thus decreasing exocarp russet accumulation in semi-russet pear
agriculture
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PAL activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 24 hours after inoculation in the resistant varieties. Defense enzymes PAL, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. PAL is induced first, followed by tyrosine ammonia-lyase and than polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
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analysis
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useful for determining Phe or removing Phe from mammalian systems
analysis
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immobilization of phenylalanine ammonia-lyase into gelatin on polyester films to determine phenylalanine in urine for the prediagnosis of phenylketonuria. Immobilized enzyme retaines 100% apparent activity after 30 days and as much as 75% of activity is retained after 2 months. The method is sufficiently sensitive to determine the phenylalanine concentration in phenylketonuric infants' urine
analysis
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an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other methods
analysis
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an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other methods
analysis
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an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other methods
analysis
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an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other methods
biotechnology
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compared to the free enzyme, the PAL-CLEA exhibit increased stability of the enzyme against various deactivating conditions such as pH, temperature, denaturants, and organic solvents and show higher storage stability than its soluble counterpart. Additionally, PAL-CLEAs can be recycled at least for 12 consecutive batch reactions without dramatic activity loss, increases the commercial potential of PAL for synthesis of L-phenylalanine
biotechnology
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the enzyme can be used for the development of dietary foods and biotechnological products for patients with phenylketonuria
drug development
AtPAL2 is a very good catalyst for the formation of 3-fluoro-L-phenylalanine, 4-fluoro-L-phenylalanine and 2-chloro-L-phenylalanine. Such noncanonical amino acids are valuable building blocks for the formation of various drug molecules
drug development
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
drug development
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
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food industry
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the enzyme can be used for the development of dietary foods and biotechnological products for patients with phenylketonuria
food industry
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the enzyme from Cyathobasis fruticulosa is a potential candidate for serial production of dietary food and biotechnological products
medicine
use of enzyme for substitution treatment of human phenylketonuria. Identification of B and T cell epitopes on the enzyme protein and covering of the immunogenic regions
medicine
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use of enzyme in therapy of human phenylketonuria. Preparation of microcapsules containing emulsified enzyme. Emulsification of enzyme solution with water-saturated ether causes no loss in activity but results in loss of protein content in the aqueous phase due to specific loss of impurities in the protein sample. Emulsification of enzyme solution with ether/ethanol mixture results in a 50% decrase in activity. Hydroxypropyl-gamma-cyclodextrin and hydroxypropyl-beta-cyclodextrin protect against emulsion mediated loss in activity
medicine
PAL activity is able to effect a reduction in phenylalanine levels and hence provide the basis of a unique therapy for human hyperphenylalaninemic patients
medicine
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the enzyme can be used as oral therapeutic, in an encapsulated form, in phenylketonuria/hyperphenylalaninemia
medicine
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enzyme substitution therapy for the treatment of phenylketonuria
medicine
enzyme substitution therapy for the treatment of phenylketonuria
medicine
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enzyme substitution therapy with the phenylalanine ammonia lyase is a new approach to the treatment of patients with phenylketonuria
medicine
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
medicine
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the 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 prolonged half-life of the mutant enzyme at 70°C, the higher resistance to a low pH of 3.5 and protease make the mutant enzyme E75L a candidate for oral medicine of phenylketonuria
medicine
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
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medicine
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the 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 prolonged half-life of the mutant enzyme at 70°C, the higher resistance to a low pH of 3.5 and protease make the mutant enzyme E75L a candidate for oral medicine of phenylketonuria
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pharmacology
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the ability of PAL to catalyze the conversion of L-Phe into nontoxic compounds in the absence of additional cofactors leads to its use as a therapeutic agent for the treatment of phenylketonuria
pharmacology
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enzyme substitution therapy for the treatment of phenylketonuria
pharmacology
enzyme substitution therapy for the treatment of phenylketonuria
pharmacology
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enzyme substitution therapy with the phenylalanine ammonia lyase is a new approach to the treatment of patients with phenylketonuria
pharmacology
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
pharmacology
the enzyme is specifically advantageous for the production of the hypertension drug 2-chloro-L-phenylalanine
pharmacology
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the 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 prolonged half-life of the mutant enzyme at 70°C, the higher resistance to a low pH of 3.5 and protease make the mutant enzyme E75L a candidate for oral medicine of phenylketonuria
pharmacology
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
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pharmacology
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the 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 prolonged half-life of the mutant enzyme at 70°C, the higher resistance to a low pH of 3.5 and protease make the mutant enzyme E75L a candidate for oral medicine of phenylketonuria
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synthesis
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production of L-phenylalanine, which is used in the manufacture of the artificial sweetener aspartame and in parenteral nutrition, it is also used as a building block for the synthesis of the macrolide antibiotic rutamycin B
synthesis
Rhodococcus rubra
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production of L-phenylalanine, which is used in the manufacture of the artificial sweetener aspartame and in parenteral nutrition, it is also used as a building block for the synthesis of the macrolide antibiotic rutamycin B
synthesis
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use of enzyme for production of enantiopure D- and L-heteroaryl-2-alanines, i.e. R- and S-2-amino-3-(heteroaryl)propanoic acids
synthesis
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phenylalanine ammonia-lyase's reverse reaction is exploited for the commercial production of optically pure L-phenylalanine from trans-cinnamic acid
synthesis
the enzyme is involved in and useful for production salidroside, an effective adaptogenic drug from the medicinal plant Rhodiola sachalinensis
synthesis
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the enzyme is useful for an economic way for biosynthesis of 15NL-phenylalanine, yield and purity of 15NL-phenylalanine reach 71% and 99.3%, respectively
synthesis
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heterologous expression of enzyme in Streptomyces lividans. After 4 days of cultivation using glucose as carbon source, the maximal level of cinnamic acid reaches 210 mg/l. When glycerol is used as carbon source az 30 g/l, the maximal level of produced cinnamic acid reaches 450 mg/l. Using raw starch, xylose or xylan as carbon source, the maximal level of cinnamic acid reaches 460, 300, and 130 mg/l, respectively
synthesis
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improvement of recombinant phenylalanine ammonia-lyase stability in Escherichia coli during the enzymatic methods of L-phenylalanine production. The optimum values for testing variables are 13.04 mM glycerol, 1.87 mM sucrose, 4.09 mM DTT, and 69 mM Mg2+. The maximum phenylalanine ammonia-lyase activity is retained as 67.73 units/g after three successive cycles of bioconversion. In comparison to initial phenylalanine ammonia-lyase activity, the loss of phenylalanine ammonia-lyase activity was only 22%. Phenylalanine ammonia-lyase activity is enhanced about 23% in comparison to the control
synthesis
AtPAL2 is a very good catalyst for the formation of 3-fluoro-L-phenylalanine, 4-fluoro-L-phenylalanine and 2-chloro-L-phenylalanine. Such noncanonical amino acids are valuable building blocks for the formation of various drug molecules
synthesis
reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including (2S)-pinocembrin, (2S)-naringenin, p-hydroxystyrene, p-coumarate, trans-cinnamic acid
synthesis
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reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including dicinnamoylmethane, 6-fluoro-dicinnamoylmethane, 6,6'-difluoro-dicinnamoylmethane or pinosylvin
synthesis
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reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including trans-cinnamic acid
synthesis
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reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including trans-cinnamic acid, (2RS)-pinocembrin, styrene, pinosylvin or (2S)-naringenin
synthesis
reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including trans-cinnamic acid, p-coumaric acid, (2RS)-pinocembrin, (2RS)-naringenin, trans-resveratrol, pinosylvin, genistein
synthesis
synthesis of analogues of L-phenylalanine, that are incorporated as pharmacophores in several peptidomimetic drug molecules and are therefore of particular interest to the fine chemical industry. Engineering of phenylalanine ammonia lyase from Rhodotorula graminis and identification of variants with very high levels of activity towards a panel of substituted cinnamic acids including; 4-bromo-, 3-bromo-, 4-fluoro-, 3-fluoro- and 3-nitro-cinnamic acid. Optimisation studies for use of one of these variants in the preparative synthesis of related variants of L-phenylalanine. Identification of variants used in a preparative scale biotransformation resulting in a 94% conversion to L-4-Br-phenylalanine (more than 99% enantiomeric excess)
synthesis
synthesis of substituted D-phenylalanines in high yield and excellent optical purity, starting from inexpensive cinnamic acids, is achieved with a one-pot approach by coupling phenylalanine ammonia lyase amination with a chemoenzymatic deracemization (based on stereoselective oxidation and nonselective reduction). A simple high-throughput solid-phase screening method is developed to identify phenylalanine ammonia lyases with higher rates of formation of non-natural D-phenylalanines. The best variants are exploited in the chemoenzymatic cascade, thus increasing the yield and enantiomeric excess value of the D-configured product
synthesis
the enzyme is specifically advantageous for the production of 2-chloro-L-phenylalanine, an important intermediate for the synthesis of angiotensin 1-converting enzyme inhibitors
synthesis
the recombinant ZmPAL2 is a good candidate for the production of trans-cinnamic acid. The recombinant ZmPAL2 can effectively catalyze L-phenylalanine to trans-cinnamic acid, and the trans-cinnamic acid concentration can reach up to 5 g/l
synthesis
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the enzyme is useful for an economic way for biosynthesis of 15NL-phenylalanine, yield and purity of 15NL-phenylalanine reach 71% and 99.3%, respectively
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synthesis
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phenylalanine ammonia-lyase's reverse reaction is exploited for the commercial production of optically pure L-phenylalanine from trans-cinnamic acid
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