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Information on EC 4.1.1.43 - phenylpyruvate decarboxylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q06408
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4.1.1.43 phenylpyruvate decarboxylaseIUBMB Comments
The enzyme from the bacterium Azospirillum brasilense also acts on some other substrates, including (indol-3-yl)pyruvate, with much lower efficiency. However, it only possesses classical Michaelis-Menten kinetics with phenylpyruvate. Aliphatic 2-oxo acids longer that 2-oxohexanoate are not substrates. cf. EC 4.1.1.74, indolepyruvate decarboxylase.
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Word Map
- 4.1.1.43
- 2-phenylethanol
- decarboxylases
- pdc5
- isobutanol
- tyrosol
-
rose-like
-
4-hydroxyphenylacetic
-
2-keto
-
fusel
- 4-hydroxyphenylpyruvate
-
diphosphate-dependent
-
isoamyl
- synthesis
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
aro10, phenylpyruvate decarboxylase, ydr380w, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Decarboxylase, phenylpyruvate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
phenylpyruvate carboxy-lyase (phenylacetaldehyde-forming)
The enzyme from the bacterium Azospirillum brasilense also acts on some other substrates, including (indol-3-yl)pyruvate, with much lower efficiency. However, it only possesses classical Michaelis-Menten kinetics with phenylpyruvate. Aliphatic 2-oxo acids longer that 2-oxohexanoate are not substrates. cf. EC 4.1.1.74, indolepyruvate decarboxylase.
CAS REGISTRY NUMBER
COMMENTARY
37289-45-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxo-4-phenylbutanoic acid
?
9% activity compared to phenylpyruvate
-
-
?
2-oxobutanoic acid
?
0.2% activity compared to phenylpyruvate
-
-
?
2-oxohexanoic acid
?
6% activity compared to phenylpyruvate
-
-
?
2-oxopentanoic acid
?
1% activity compared to phenylpyruvate
-
-
?
3-methyl-2-oxobutanoic acid
?
1% activity compared to phenylpyruvate
-
-
?
3-methyl-2-oxopentanoic acid
?
2% activity compared to phenylpyruvate
-
-
?
4-hydroxyphenylpyruvate
4-hydroxyphenylacetaldehyde + CO2
63% activity compared to phenylpyruvate
-
-
?
4-methyl-2-oxopentanoic acid
?
6% activity compared to phenylpyruvate
-
-
?
4-methylthio-2-oxobutanoic acid
?
6% activity compared to phenylpyruvate
-
-
?
benzoylformic acid
?
0.2% activity compared to phenylpyruvate
-
-
?
indole-3-pyruvate
indoleacetaldehyde + CO2
preferred substrate, 100% activity
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
preferred substrate, 100% activity
-
-
?
pyruvic acid
?
0.02% activity compared to phenylpyruvate
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
first step in the Ehrlich pathway
-
?
additional information
?
-
PPDC is essentially unable to utilize pyruvate and 3-indoleglyoxylic acid
-
-
?
additional information
?
-
-
PPDC is essentially unable to utilize pyruvate and 3-indoleglyoxylic acid
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Phenylpyruvate
Phenylacetaldehyde + CO2
-
first step in the Ehrlich pathway
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
2-oxo-4-phenylbutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
8.5
3-methyl-2-oxobutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
3.1
3-methyl-2-oxopentanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.09
4-hydroxyphenylpyruvate
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.9
4-methyl-2-oxopentanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.64
4-methylthio-2-oxobutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.03
Indole-3-pyruvate
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
5.5
2-oxobutanoic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
6.4
2-oxobutanoic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
7
2-oxobutanoic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
7.6
2-oxobutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.17
2-oxohexanoic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.46
2-oxohexanoic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.55
2-oxohexanoic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.69
2-oxohexanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
1
2-oxohexanoic acid
mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.37
2-oxopentanoic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.54
2-oxopentanoic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.63
2-oxopentanoic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.96
2-oxopentanoic acid
mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
2.1
2-oxopentanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.054
phenylpyruvate
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.1
phenylpyruvate
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.18
phenylpyruvate
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.8
phenylpyruvate
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
5.5
Pyruvic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
6.4
Pyruvic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
9.7
Pyruvic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
25
Pyruvic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
2-oxo-4-phenylbutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
19
3-methyl-2-oxobutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
11
3-methyl-2-oxopentanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
11
4-hydroxyphenylpyruvate
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
10
4-methyl-2-oxopentanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
7.7
4-methylthio-2-oxobutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.04
2-oxobutanoic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.06
2-oxobutanoic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
2.2
2-oxobutanoic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
3.9
2-oxobutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.41
2-oxohexanoic acid
mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.96
2-oxohexanoic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
1.3
2-oxohexanoic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
3.3
2-oxohexanoic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
8.8
2-oxohexanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.39
2-oxopentanoic acid
mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.76
2-oxopentanoic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
2
2-oxopentanoic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
2.1
2-oxopentanoic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
5.2
2-oxopentanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.14
Indole-3-pyruvate
mutant enzyme E545L, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
5.4
Indole-3-pyruvate
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.85
phenylpyruvate
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
1.2
phenylpyruvate
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
4.8
phenylpyruvate
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
8.8
phenylpyruvate
mutant enzyme E545L, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
20
phenylpyruvate
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.064
Pyruvic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.32
Pyruvic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.34
Pyruvic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.45
Pyruvic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19
2-oxo-4-phenylbutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
2.2
3-methyl-2-oxobutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
3.5
3-methyl-2-oxopentanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
125
4-hydroxyphenylpyruvate
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
11
4-methyl-2-oxopentanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
12
4-methylthio-2-oxobutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.35
benzoylformic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
200
Indole-3-pyruvate
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.007
2-oxobutanoic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.009
2-oxobutanoic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.315
2-oxobutanoic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.52
2-oxobutanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.42
2-oxohexanoic acid
mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
2.8
2-oxohexanoic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
5.8
2-oxohexanoic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
6
2-oxohexanoic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
13
2-oxohexanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.4
2-oxopentanoic acid
mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
2.1
2-oxopentanoic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
2.5
2-oxopentanoic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
3.4
2-oxopentanoic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
3.7
2-oxopentanoic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.03
phenylpyruvate
mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
1.1
phenylpyruvate
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
200
phenylpyruvate
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.003
Pyruvic acid
mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.027
Pyruvic acid
mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.035
Pyruvic acid
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.06
Pyruvic acid
mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
0.07
Pyruvic acid
mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E545L
the mutant shows 730fold decrease in kcat (phenylpyruvate) and 38fold decrease in kcat (indole-3-pyruvate) compared to the wild type enzyme
I335Y
compared to the wild type enzyme, the mutant exhibits 0.6% catalytic efficiency with phenylpyruvate, 33% catalytic efficiency with 2-oxohexanoic acid, 213% catalytic efficiency with 2-oxopentanoic acid, 1.7% catalytic efficiency with 2-oxobutanoic acid, and 7% catalytic efficiency with pyruvic acid
I335Y/M624W
compared to the wild type enzyme, the mutant exhibits 0.02% catalytic efficiency with phenylpyruvate, 2.3% catalytic efficiency with 2-oxohexanoic acid, 25% catalytic efficiency with 2-oxopentanoic acid, no activity with 2-oxobutanoic acid, and 59% catalytic efficiency with pyruvic acid
M624W
compared to the wild type enzyme, the mutant exhibits 3.4% catalytic efficiency with phenylpyruvate, 32% catalytic efficiency with 2-oxohexanoic acid, 131% catalytic efficiency with 2-oxopentanoic acid, 1.4% catalytic efficiency with 2-oxobutanoic acid, and 152% catalytic efficiency with pyruvic acid
Q448W
compared to the wild type enzyme, the mutant exhibits 45% catalytic efficiency with phenylpyruvate, 16% catalytic efficiency with 2-oxohexanoic acid, 231% catalytic efficiency with 2-oxopentanoic acid, 62% catalytic efficiency with 2-oxobutanoic acid, and 130% catalytic efficiency with pyruvic acid
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
overexpression of phenylpyruvate decarboxylase ARO10 and alcoholdehydrogenase ADH2 genes of Saccharomyces cerevisiae in Kluyveromyces marxianus results in synthesis of 1 g/l 2-phenylethanol
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vuralhan, Z.; Morais, M.A.; Tai, S.L.; Piper, M.D.; Pronk, J.T.
Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae
Appl. Environ. Microbiol.
69
4534-4541
2003
Saccharomyces cerevisiae
Hwang, J.Y.; Park, J.; Seo, J.H.; Cha, M.; Cho, B.K.; Kim, J.; Kim, B.G.
Simultaneous synthesis of 2-phenylethanol and L-homophenylalanine using aromatic transaminase with yeast Ehrlich pathway
Biotechnol. Bioeng.
102
1323-1329
2008
Saccharomyces cerevisiae
Kneen, M.; Stan, R.; Yep, A.; Tyler, R.; Saehuan, C.; McLeish, M.
Characterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae
FEBS J.
278
1842-1853
2011
Saccharomyces cerevisiae (Q06408), Saccharomyces cerevisiae
Kim, T.; Lee, S.; Oh, M.
Biosynthesis of 2-phenylethanol from glucose with genetically engineered Kluyveromyces marxianus
Enzyme Microb. Technol.
61-62
44-47
2014
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH499
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