Information on EC 4.1.1.43 - phenylpyruvate decarboxylase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.1.1.43
-
RECOMMENDED NAME
GeneOntology No.
phenylpyruvate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phenylpyruvate = phenylacetaldehyde + CO2
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-phenylalanine degradation II (anaerobic)
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L-phenylalanine degradation III
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Metabolic pathways
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Phenylalanine metabolism
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Tryptophan metabolism
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methionine metabolism
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phenylalanine metabolism
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SYSTEMATIC NAME
IUBMB Comments
phenylpyruvate carboxy-lyase (phenylacetaldehyde-forming)
Also acts on (indol-3-yl)pyruvate.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-45-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Achromobacter eurydice
SC 16386
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Manually annotated by BRENDA team
Achromobacter eurydice SC 16386
SC 16386
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Manually annotated by BRENDA team
other name: Achromobacter eurydice
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain 47
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Manually annotated by BRENDA team
strain 47
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-
Manually annotated by BRENDA team
no activity in Pseudomonas fluorescens
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-
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Manually annotated by BRENDA team
no activity in Pseudomonas fluorescens Psd
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-
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Manually annotated by BRENDA team
strain 239
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-
Manually annotated by BRENDA team
strain 239
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Manually annotated by BRENDA team
SC 13940, SC 13914, SC 16157, SC 16154, SC 16012, SC 16376, SC 16013
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Manually annotated by BRENDA team
SC 16387
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Manually annotated by BRENDA team
SC 16387
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-ketohexanoic acid
pentanal + CO2
show the reaction diagram
-
1% activity compared to phenylpyruvate
-
-
-
2-oxo-4-phenylbutanoic acid
?
show the reaction diagram
9% activity compared to phenylpyruvate
-
-
?
2-Oxo-gamma-ethylthiobutanoate
beta-Ethiopropanal + CO2
show the reaction diagram
2-Oxo-isohexanoate
?
show the reaction diagram
-
at approximately 5% of the activity with phenylpyruvate
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-
-
2-oxobutanoic acid
?
show the reaction diagram
0.2% activity compared to phenylpyruvate
-
-
?
2-Oxohexanoate
Pentanal + CO2
show the reaction diagram
2-oxohexanoic acid
?
show the reaction diagram
6% activity compared to phenylpyruvate
-
-
?
2-oxopentanoic acid
?
show the reaction diagram
1% activity compared to phenylpyruvate
-
-
?
3-methyl-2-oxobutanoic acid
?
show the reaction diagram
1% activity compared to phenylpyruvate
-
-
?
3-methyl-2-oxopentanoic acid
?
show the reaction diagram
2% activity compared to phenylpyruvate
-
-
?
4-hydroxyphenylpyruvate
4-hydroxyphenylacetaldehyde + CO2
show the reaction diagram
63% activity compared to phenylpyruvate
-
-
?
4-methyl-2-oxopentanoic acid
?
show the reaction diagram
6% activity compared to phenylpyruvate
-
-
?
4-methylthio-2-oxobutanoate
beta-methiopropanal + CO2
show the reaction diagram
4-methylthio-2-oxobutanoic acid
?
show the reaction diagram
6% activity compared to phenylpyruvate
-
-
?
4-phenyl-2-oxobutanoic acid
3-phenylpropanal + CO2
show the reaction diagram
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2.3% activity compared to phenylpyruvate
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-
?
5-phenyl-2-oxopentanoic acid
4-phenylbutanal + CO2
show the reaction diagram
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110% activity compared to phenylpyruvate
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benzoylformic acid
?
show the reaction diagram
0.2% activity compared to phenylpyruvate
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-
?
indole-3-pyruvate
indole-3-acetate + CO2
show the reaction diagram
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10.4% activity compared to phenylpyruvate
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-
?
indole-3-pyruvate
indoleacetaldehyde + CO2
show the reaction diagram
preferred substrate, 100% activity
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?
indole-3-pyruvic acid + acetaldehyde
3-hydroxy-1-(3-indoyl)-2-butanone
show the reaction diagram
Achromobacter eurydice
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-
-
?
indolepyruvate
indoleacetaldehyde + CO2
show the reaction diagram
Indolepyruvate
Indoleethanal + CO2
show the reaction diagram
L-phenylalanine
phenylacetic acid + CO2
show the reaction diagram
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-
-
-
?
L-tryptophan
indole-acetic acid + CO2
show the reaction diagram
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-
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-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
show the reaction diagram
phenylpyruvate + acetaldehyde
3-hydoxy-1-phenyl-2-butanone
show the reaction diagram
phenylpyruvate + acetaldehyde
3-hydroxy-1-phenyl-2-butanone
show the reaction diagram
phenylpyruvate + n-butyraldehyde
3-hydroxy-1-phenyl-2-hexanone
show the reaction diagram
phenylpyruvate + pentanal
3-hydroxy-1-phenyl-2-heptanone
show the reaction diagram
phenylpyruvate + propionaldehyde
3-hydroxy-1-phenyl-2-pentanone
show the reaction diagram
pyruvic acid
?
show the reaction diagram
0.02% activity compared to phenylpyruvate
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Phenylpyruvate
Phenylacetaldehyde + CO2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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can partially replace Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(1-hydroxyethyl)-3-deaza-thiamine diphosphate
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3-deaza-thiamine diphosphate
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p-hydroxyphenylpyruvate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.51
2-ketohexanoic acid
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in 10 mM MES, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate, 0.35 mM NADH, and 0.125 units alcohol dehydrogenase, at pH 6.5 and 30C
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 30C
5.5 - 7.6
2-oxobutanoic acid
0.17 - 1
2-oxohexanoic acid
0.37 - 2.1
2-Oxopentanoic acid
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 30C
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 30C
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 30C
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 30C
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 30C
1.91
4-phenyl-2-oxobutanoic acid
-
in 10 mM MES, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate, 0.35 mM NADH, and 0.125 units alcohol dehydrogenase, at pH 6.5 and 30C
0.3
5-phenyl-2-oxopentanoic acid
-
in 10 mM MES, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate, 0.35 mM NADH, and 0.125 units alcohol dehydrogenase, at pH 6.5 and 30C
0.03 - 0.13
Indole-3-pyruvate
0.0051 - 1.08
phenylpyruvate
5.5 - 25
Pyruvic acid
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29
2-ketohexanoic acid
Azospirillum brasilense
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in 10 mM MES, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate, 0.35 mM NADH, and 0.125 units alcohol dehydrogenase, at pH 6.5 and 30C
1.7
2-oxo-4-phenylbutanoic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
0.04 - 3.9
2-oxobutanoic acid
0.41 - 8.8
2-oxohexanoic acid
0.39 - 5.2
2-Oxopentanoic acid
19
3-methyl-2-oxobutanoic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
11
3-methyl-2-oxopentanoic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
11
4-hydroxyphenylpyruvate
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
10
4-methyl-2-oxopentanoic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
7.7
4-methylthio-2-oxobutanoic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
0.21
4-phenyl-2-oxobutanoic acid
Azospirillum brasilense
-
in 10 mM MES, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate, 0.35 mM NADH, and 0.125 units alcohol dehydrogenase, at pH 6.5 and 30C
1.7
5-phenyl-2-oxopentanoic acid
Azospirillum brasilense
-
in 10 mM MES, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate, 0.35 mM NADH, and 0.125 units alcohol dehydrogenase, at pH 6.5 and 30C
0.07 - 5.4
Indole-3-pyruvate
0.85 - 20
phenylpyruvate
0.064 - 0.45
Pyruvic acid
additional information
phenylpyruvate
Azospirillum brasilense
-
in 10 mM MES, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate, 0.35 mM NADH, and 0.125 units alcohol dehydrogenase, at pH 6.5 and 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19
2-oxo-4-phenylbutanoic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
7642
0.007 - 0.52
2-oxobutanoic acid
5386
0.42 - 13
2-oxohexanoic acid
2682
0.4 - 3.7
2-Oxopentanoic acid
2879
2.2
3-methyl-2-oxobutanoic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
3156
3.5
3-methyl-2-oxopentanoic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
3009
125
4-hydroxyphenylpyruvate
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
423
11
4-methyl-2-oxopentanoic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
2785
12
4-methylthio-2-oxobutanoic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
13262
0.35
benzoylformic acid
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
3710
200
Indole-3-pyruvate
Saccharomyces cerevisiae
Q06408
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30C
2408
0.03 - 200
phenylpyruvate
198
0.003 - 0.07
Pyruvic acid
1725
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Achromobacter eurydice
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
Achromobacter eurydice
-
1 * 90000 + 1 * 40000, SDS-PAGE
56800
-
4 * 56800, SDS-PAGE
57000
x * 57000, SDS-PAGE
58000
-
4 * 58000, X-ray crystallography, asymmetric dimer of dimers, in the asymmetric unit two subunits of PPDC are tightly packed to form a dimer related by noncrystallographic two-fold symmetry
60000
-
4 * 60000, gel filtration
90000
Achromobacter eurydice
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1 * 90000 + 1 * 40000, SDS-PAGE
150000
Achromobacter eurydice
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gel filtration
240600
-
gel filtration, recombinant enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 57000, SDS-PAGE
homotetramer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method with 15% polyethylene glycol 4000 (w/v), 10% glycerol (v/v) in 100 mM HEPES buffer, pH 7.0
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hanging drop vapour diffusion method with precipitant solution containing 15% PEG4000 (w /v), 10% glycerol (v /v) in 100 mM HEPES buffer pH 7.5, at 20C
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
30C, 1 h, about 60% loss of activity
4563
6.3 - 6.4
-
30C, 1 h, completely stable, maximal stability
4563
8.8
-
30C, 1 h, 80% loss of activity
4563
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
thiamine diphosphate stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 64 days, no change in activity
Achromobacter eurydice
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap HP column chromatography and Superdex G200 gel filtration
-
Ni-nitrilotriacetic acid affinity chromatography and Superdex-200 gel filtration
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Ni-NTA column chromatography
partial
Achromobacter eurydice
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli Bl21-CodonPlus (DE3)-RP cells
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expressed in Escherichia coli BL21-CodonPlus(DE3)-RP cells
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expressed in Escherichia coli DHP3 and DHP4 cells
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expressed in Saccharomyces cerevisiae strain IMZ245
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced by L-phenylalanine
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
-
an ipdC-knockout mutant produces only 10% (w/v) of the wild type indole-3-acetic acid production level