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Information on EC 4.1.1.76 - arylmalonate decarboxylase and Organism(s) Bordetella bronchiseptica and UniProt Accession Q05115

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.76 arylmalonate decarboxylase
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Select one or more organisms in this record: ?
This record set is specific for:
Bordetella bronchiseptica
UNIPROT: Q05115 not found.
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The taxonomic range for the selected organisms is: Bordetella bronchiseptica
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
amdase, arylmalonate decarboxylase, aryl/alkenyl malonate decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Arylmalonate decarboxylase
-
AMDase
aryl/alkenyl malonate decarboxylase
-
-
Arylmalonate decarboxylase
Arylmalonate decarboxylase (Alcaligenes bronchisepticus strain KU 1201)
-
-
-
-
Decarboxylase, arylmalonate
-
-
-
-
Decarboxylase, arylmalonate (Bordetella bronchiseptica clone pAMD100 reduced)
-
-
-
-
Decarboxylase, arylmalonate (Bordetella bronchiseptica strain KU1201 reduced)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-aryl-2-methylmalonate = 2-arylpropanoate + CO2
show the reaction diagram
a hydrophobic interaction between the enzyme and its substrate via their aromatic rings is especially important for the enzyme function
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
decarboxylation
SYSTEMATIC NAME
IUBMB Comments
2-aryl-2-methylmalonate carboxy-lyase (2-arylpropanoate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
144713-36-0
-
154102-95-1
decarboxylase, arylmalonate (Bordetella bronchiseptica strain KU1201 reduced) /arylmalonate decarboxylase (Alcaligenes bronchisepticus strain KU 1201) /decarboxylase, arylmalonate (Bordetella bronchiseptica clone pAMD100 reduced)
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1-benzothiophen-5-yl)(hydroxy)propanedioic acid
(2R)-(1-benzothiophen-5-yl)(hydroxy)acetic acid + CO2
show the reaction diagram
-
-
-
?
(1E)-but-1-en-1-yl(methyl)propanedioic acid
(2S,3Z)-2-methylhex-3-enoic acid + CO2
show the reaction diagram
-
-
-
?
(6-methoxynaphthalen-2-yl)(methyl)propanedioic acid
(R)-2-(6-methoxynaphthalen-2-yl)-2-methylpropanoic acid + CO2
show the reaction diagram
-
-
-
?
2(thien-2-yl) malonate
? + CO2
show the reaction diagram
-
-
-
?
2-(2-fluoro-4-biphenyl)-2-methylmalonate
(R)-2-methyl-2-(2-fluoro-4-biphenyl)propionate + CO2
show the reaction diagram
-
-
-
?
2-(2-fluoro-4-biphenyl)-2-methylmalonate
(S)-2-methyl-2-(2-fluoro-4-biphenyl)propionate + CO2
show the reaction diagram
-
-
-
?
2-(furan-2-yl) malonic acid
(furan-2-yl)acetic acid + CO2
show the reaction diagram
-
-
-
?
2-amino-2-vinylmalonate
(R)-vinylglycine + CO2
show the reaction diagram
-
-
-
?
2-aminophenylmalonate
?
show the reaction diagram
-
-
-
?
2-aryl-2-methylmalonate
(2R)-arylpropionate + CO2
show the reaction diagram
-
-
-
?
2-aryl-2-methylmalonate
2-arylpropionate + CO2
show the reaction diagram
2-hydroxy-2-phenylmalonic acid
(2S)-hydroxy(phenyl)ethanoic acid + CO2
show the reaction diagram
-
-
-
?
2-hydroxy-2-phenylmalonic acid
? + CO2
show the reaction diagram
-
-
-
?
2-hydroxymalonate
?
show the reaction diagram
-
-
-
?
2-methyl-2-(naphthalen-2-yl)malonate
2-(naphthalen-2-yl)propionate + CO2
show the reaction diagram
-
-
-
?
2-methyl-2-(thien-2-yl)malonate
2-(thien-2-yl)propionate + CO2
show the reaction diagram
-
-
-
?
2-methyl-2-phenylmalonate
2-phenylpropanoate + CO2
show the reaction diagram
2-methyl-2-vinylmalonic acid
(2S)-2-methylbut-3-enoic acid + CO2
show the reaction diagram
for the small 2-methyl-2-vinylmalonate substrate, both the binding and the following transition states contribute to the enantioselectivity
-
-
?
2-phenyl-2-methylmalonate
(2R)-phenylpropionate + CO2
show the reaction diagram
-
-
-
?
2-phenylmalonate
2-phenylacetate + CO2
show the reaction diagram
-
-
-
?
2-vinyl-2-methylmalonic acid
(2S)-2-methylbut-3-enoic acid + CO2
show the reaction diagram
-
-
-
?
2-vinyl-2-methylmalonic acid
? + CO2
show the reaction diagram
-
-
-
?
alpha-aryl-alpha-methylmalonate
alpha-arylpropionate + CO2
show the reaction diagram
-
-
-
?
amino(phenyl)propanedioic acid
(2S)-amino(phenyl)ethanoic acid + CO2
show the reaction diagram
-
-
-
?
hydroxy(2-methylprop-1-en-1-yl)propanedioic acid
(2S)-2-hydroxy-4-methylpent-3-enoic acid + CO2
show the reaction diagram
-
-
-
?
hydroxy(pyridin-3-yl)propanedioic acid
(2R)-hydroxy(pyridin-3-yl)acetic acid + CO2
show the reaction diagram
-
-
-
?
hydroxy(thiophen-2-yl)propanedioic acid
(2S)-hydroxy(thiophen-2-yl)acetic acid + CO2
show the reaction diagram
-
-
-
?
hydroxy[(1E)-prop-1-en-1-yl]propanedioic acid
(2S)-2-hydroxybut-3-enoic acid + CO2
show the reaction diagram
-
-
-
?
methyl(2-methylprop-1-en-1-yl)propanedioic acid
(2S)-2,4-dimethylpent-3-enoic acid + CO2
show the reaction diagram
-
-
-
?
methyl(naphthalen-2-yl)propanedioic acid
(R)-2-methyl-2-(naphthalen-2-yl)propanoic acid + CO2
show the reaction diagram
-
-
-
?
methyl(phenyl)propanedioic acid
(2R)-2-phenylpropanoic acid + CO2
show the reaction diagram
-
-
-
?
methyl(phenyl)propanedioic acid
(2S)-2-phenylpropanoic acid + CO2
show the reaction diagram
-
-
-
?
methyl[(1E)-prop-1-en-1-yl]propanedioic acid
(2S,3Z)-2-methylpent-3-enoic acid + CO2
show the reaction diagram
-
-
-
?
Phenylmalonate
Phenylacetate + CO2
show the reaction diagram
(1-benzofuran-2-yl)(hydroxy)propanedioic acid + H+
(2R)-(1-benzofuran-2-yl)(hydroxy)acetic acid + CO2
show the reaction diagram
93% yield
-
-
?
(1-benzothiophen-6-yl)(hydroxy)propanedioic acid + H+
(2R)-(1-benzothiophen-6-yl)(hydroxy)acetic acid + CO2
show the reaction diagram
89% yield
-
-
?
(4,5-dimethylfuran-2-yl)(hydroxy)propanedioic acid + H+
(2R)-(4,5-dimethylfuran-2-yl)(hydroxy)acetic acid + CO2
show the reaction diagram
96% yield
-
-
?
(furan-2-yl)(hydroxy)propanedioic acid + H+
(2R)-(furan-2-yl)(hydroxy)acetic acid + CO2
show the reaction diagram
95% yield
-
-
?
1-Naphthylmalonate
?
show the reaction diagram
-
-
-
-
?
2-(2-fluoro-4-biphenyl)-2-methylmalonate
(R)-alpha-methyl-alpha-(2-fluoro-4-biphenyl)propionate + CO2
show the reaction diagram
-
-
trivial name (R)flurbiprofen, 92% enantiomeric excess
?
2-aryl-2-methylmalonate
2-arylpropionate + CO2
show the reaction diagram
-
-
-
?
2-aryl-2-methylmalonate + H+
2-arylpropionate + CO2
show the reaction diagram
-
-
-
?
2-Naphthylmalonate
?
show the reaction diagram
-
-
-
-
?
2-phenyl-2-fluoromalonate
(R)-alpha-fluorophenylacetic acid + CO2
show the reaction diagram
-
-
99% enantiomeric excess
?
2-phenyl-2-methylmalonate
(2R)-phenylpropionate + CO2
show the reaction diagram
2-Thienylmalonate
?
show the reaction diagram
-
-
-
-
?
alpha-Methyl-alpha(2-thienyl)malonate
?
show the reaction diagram
-
-
-
-
?
alpha-methyl-alpha-(alpha-thienyl)malonate
alpha-(alpha-thienyl)propionate + CO2
show the reaction diagram
alpha-methyl-alpha-(beta-naphthyl)malonate
alpha-(beta-naphthyl) propionate + CO2
show the reaction diagram
alpha-methyl-alpha-(beta-naphthyl)malonate
alpha-(beta-naphthyl)propionate + CO2
show the reaction diagram
-
-
-
-
?
alpha-Methyl-alpha-phenylmalonate
?
show the reaction diagram
-
-
-
-
?
alpha-phenylbutyrate
?
show the reaction diagram
-
23% activity compared to phenylmalonate, mutant enzyme G74C
-
-
?
hydroxy(4-methylfuran-2-yl)propanedioic acid + H+
(2R)-hydroxy(4-methylfuran-2-yl)acetic acid + CO2
show the reaction diagram
995% yield
-
-
?
hydroxy(5-methoxyfuran-2-yl)propanedioic acid + H+
(2R)-hydroxy(5-methoxyfuran-2-yl)acetic acid + CO2
show the reaction diagram
84% yield
-
-
?
hydroxy(5-methylfuran-2-yl)propanedioic acid + H+
(2R)-hydroxy(5-methylfuran-2-yl)acetic acid + CO2
show the reaction diagram
95% yield
-
-
?
hydroxy(phenyl)propanedioic acid + H+
hydroxy(phenyl)acetic acid + CO2
show the reaction diagram
hydroxy(pyridin-3-yl)propanedioic acid + H+
(2R)-hydroxy(pyridin-3-yl)acetic acid + CO2
show the reaction diagram
97% yield
-
-
?
hydroxy(thiophen-2-yl)propanedioic acid + H+
(2S)-hydroxy(thiophen-2-yl)acetic acid + CO2
show the reaction diagram
97% yield
-
-
?
m-Chlorophenylmalonate
?
show the reaction diagram
-
-
-
-
?
m-Fluorophenylmalonate
?
show the reaction diagram
-
-
-
-
?
mandelate
?
show the reaction diagram
-
14% activity compared to phenylmalonate, mutant enzyme G74C
-
-
?
methyl(2-naphthyl)malonic acid
(2R)-2-(2-naphthyl)propanoic acid + CO2
show the reaction diagram
-
-
-
-
?
methyl(2-thienyl)malonic acid
(2S)-2-(2-thienyl)propanoic acid + CO2
show the reaction diagram
-
-
-
-
?
o-Chlorophenylmalonate
?
show the reaction diagram
-
-
-
-
?
o-Fluorophenylmalonate
?
show the reaction diagram
-
-
-
-
?
p-Chlorophenylmalonate
?
show the reaction diagram
-
-
-
-
?
p-Fluorophenylmalonate
?
show the reaction diagram
-
-
-
-
?
p-Methoxyphenylmalonate
?
show the reaction diagram
-
-
-
-
?
p-Methylphenylmalonate
?
show the reaction diagram
-
-
-
-
?
phenylglycine
?
show the reaction diagram
-
5% activity compared to phenylmalonate, mutant enzyme G74C
-
-
?
Phenylmalonate
Phenylacetate + CO2
show the reaction diagram
[2-(2-oxoethyl)phenyl]propanedioate
2-hydroxy-2,3-dihydro-1H-indene-1-carboxylate + CO2
show the reaction diagram
-
aldole reaction
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-aminophenylmalonate
?
show the reaction diagram
-
-
-
?
2-aryl-2-methylmalonate
2-arylpropionate + CO2
show the reaction diagram
2-hydroxymalonate
?
show the reaction diagram
-
-
-
?
2-phenylmalonate
2-phenylacetate + CO2
show the reaction diagram
-
-
-
?
alpha-aryl-alpha-methylmalonate
alpha-arylpropionate + CO2
show the reaction diagram
-
-
-
?
2-aryl-2-methylmalonate
2-arylpropionate + CO2
show the reaction diagram
-
-
-
?
2-aryl-2-methylmalonate + H+
2-arylpropionate + CO2
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-Bromophenylacetic acid
-
benzylphosphonate
competitive inhibitor of AMDase
3-Fluorophenylmethanephosphonic acid
-
-
alpha-Bromophenylacetic acid
-
-
Sulfhydryl agents
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.82 - 3.1
(1-benzothiophen-5-yl)(hydroxy)propanedioic acid
14.4
(1E)-but-1-en-1-yl(methyl)propanedioic acid
wild type enzyme
10.1
2-(furan-2-yl) malonic acid
wild-type, pH not specified in the publication, temperature not specified in the publication
10.4 - 18.3
2-aryl-2-methylmalonate
4.1 - 30.2
2-hydroxy-2-phenylmalonic acid
26.9
2-methyl-2-phenylmalonate
-
3.3 - 7.5
2-phenylmalonate
0.8 - 7.8
2-vinyl-2-methylmalonic acid
7.3
hydroxy(2-methylprop-1-en-1-yl)propanedioic acid
wild type enzyme
6.4 - 13
hydroxy(pyridin-3-yl)propanedioic acid
2.2 - 4.3
hydroxy(thiophen-2-yl)propanedioic acid
9.1
hydroxy[(1E)-prop-1-en-1-yl]propanedioic acid
wild type enzyme
3.5
methyl(2-methylprop-1-en-1-yl)propanedioic acid
wild type enzyme
26.9
methyl(phenyl)propanedioic acid
wild type enzyme
12.8
methyl[(1E)-prop-1-en-1-yl]propanedioic acid
wild type enzyme
0.3 - 12.1
Phenylmalonate
8.2
(1-benzofuran-2-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
3.1
(1-benzothiophen-6-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
12.7
(4,5-dimethylfuran-2-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
8.6
(furan-2-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
6.09
1-Naphthylmalonate
-
-
19.4
2-Naphthylmalonate
-
-
9.9 - 10.7
2-phenyl-2-methylmalonate
87.4
2-Thienylmalonate
-
-
12.5
alpha-Methyl-alpha(2-thienyl)malonate
-
-
1.01 - 14.3
alpha-methyl-alpha-(alpha-thienyl)malonate
0.43 - 1.25
alpha-methyl-alpha-(beta-naphthyl)malonate
25.5
alpha-methyl-alpha-phenylmalonate
-
-
4.3 - 13.3
alpha-phenylmalonate
13.3
hydroxy(4-methylfuran-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
16.1
hydroxy(5-methoxyfuran-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
9.8
hydroxy(5-methylfuran-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
30.2
hydroxy(phenyl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
6.4
hydroxy(pyridin-3-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
4.3
hydroxy(thiophen-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
9.84
m-Chlorophenylmalonate
-
-
35.7
m-Fluorophenylmalonate
-
-
0.43 - 1.56
methyl(2-naphthyl)malonic acid
5.03 - 14.5
methyl(2-thienyl)malonic acid
12.6
o-Chlorophenylmalonate
-
-
27.5
o-Fluorophenylmalonate
-
-
8.32
p-Chlorophenylmalonate
-
-
13.5
p-Fluorophenylmalonate
-
-
9.36
p-Methoxyphenylmalonate
-
-
8.89
p-methylphenylmalonate
-
-
10 - 13.9
Phenylmalonate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
54.8 - 147.7
(1-benzothiophen-5-yl)(hydroxy)propanedioic acid
23.9
(1E)-but-1-en-1-yl(methyl)propanedioic acid
wild type enzyme
0.022 - 0.27
2-aryl-2-methylmalonate
23.4 - 101
2-hydroxy-2-phenylmalonic acid
279
2-methyl-2-phenylmalonate
-
0.02 - 260
2-phenylmalonate
20.8 - 42.8
2-vinyl-2-methylmalonic acid
20.7
hydroxy(2-methylprop-1-en-1-yl)propanedioic acid
wild type enzyme
42.2 - 224.8
hydroxy(pyridin-3-yl)propanedioic acid
34 - 165.9
hydroxy(thiophen-2-yl)propanedioic acid
47.6
hydroxy[(1E)-prop-1-en-1-yl]propanedioic acid
wild type enzyme
5.2
methyl(2-methylprop-1-en-1-yl)propanedioic acid
wild type enzyme
279
methyl(phenyl)propanedioic acid
wild type enzyme
46.2
methyl[(1E)-prop-1-en-1-yl]propanedioic acid
wild type enzyme
246 - 1143
Phenylmalonate
277.9
(1-benzofuran-2-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
147.7
(1-benzothiophen-6-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
12.4
(4,5-dimethylfuran-2-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
61.9
(furan-2-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
576
1-Naphthylmalonate
-
-
1730
2-Naphthylmalonate
-
-
316 - 358
2-phenyl-2-methylmalonate
5320
2-Thienylmalonate
-
-
200
alpha-Methyl-alpha(2-thienyl)malonate
-
-
0.08 - 200
alpha-methyl-alpha-(alpha-thienyl)malonate
0.05 - 30.9
alpha-methyl-alpha-(beta-naphthyl)malonate
29.8
alpha-methyl-alpha-phenylmalonate
-
-
0.62 - 366
alpha-phenylmalonate
42.4
hydroxy(4-methylfuran-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
30.5
hydroxy(5-methoxyfuran-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
37.1
hydroxy(5-methylfuran-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
101
hydroxy(phenyl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
224.8
hydroxy(pyridin-3-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
165.9
hydroxy(thiophen-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
1420
m-Chlorophenylmalonate
-
-
2180
m-Fluorophenylmalonate
-
-
0.12 - 31
methyl(2-naphthyl)malonic acid
0.34 - 200
methyl(2-thienyl)malonic acid
1090
o-Chlorophenylmalonate
-
-
666
o-Fluorophenylmalonate
-
-
782
p-Chlorophenylmalonate
-
-
195
p-Fluorophenylmalonate
-
-
92
p-Methoxyphenylmalonate
-
-
125
p-methylphenylmalonate
-
-
12.4 - 353
Phenylmalonate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.9 - 66.6
(1-benzothiophen-5-yl)(hydroxy)propanedioic acid
1.7
(1E)-but-1-en-1-yl(methyl)propanedioic acid
wild type enzyme
0.0019 - 0.026
2-aryl-2-methylmalonate
3.3 - 6.6
2-hydroxy-2-phenylmalonic acid
0.0027 - 50
2-phenylmalonate
5.5 - 25.2
2-vinyl-2-methylmalonic acid
2.8
hydroxy(2-methylprop-1-en-1-yl)propanedioic acid
wild type enzyme
3.2 - 35.3
hydroxy(pyridin-3-yl)propanedioic acid
15.2 - 38.6
hydroxy(thiophen-2-yl)propanedioic acid
5.2
hydroxy[(1E)-prop-1-en-1-yl]propanedioic acid
wild type enzyme
1.5
methyl(2-methylprop-1-en-1-yl)propanedioic acid
wild type enzyme
10.4
methyl(phenyl)propanedioic acid
wild type enzyme
3.6
methyl[(1E)-prop-1-en-1-yl]propanedioic acid
wild type enzyme
29.6 - 1499
Phenylmalonate
33.9
(1-benzofuran-2-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
48.3
(1-benzothiophen-6-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
1
(4,5-dimethylfuran-2-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
6.4
(furan-2-yl)(hydroxy)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
29.53 - 36.16
2-phenyl-2-methylmalonate
3.2
hydroxy(4-methylfuran-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
1.9
hydroxy(5-methoxyfuran-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
3.8
hydroxy(5-methylfuran-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
3.3
hydroxy(phenyl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
35.3
hydroxy(pyridin-3-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
38.6
hydroxy(thiophen-2-yl)propanedioic acid
wild type enzyme, pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.2
benzylphosphonate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
-
mutant enzyme G74C/C188S, pH 8.5, 37°C
0.07
-
mutant enzyme S71C/C188S, pH 8.5, 37°C
1.3
-
mutant enzyme C188S, pH 8.5, 37°C
467
-
wild type enzyme, pH 8.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
activity of mutant enzyme C188S retains maximal activity from pH 6.0 to pH 11., substrate: phenylmalonate
8
wild-type enzyme, substrate: phenylmalonate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
pH 5.0: about 50% of maximal activity, pH 9.5: about 55% of maximal activity, substrate: phenylmalonate, wild-type enzyme
6 - 11
activity of mutant enzyme C188S retains maximal activity from pH 6.0 to pH 11.0, substrate: phenylmalonate
6 - 9
-
pH 6.0: about 55% of maximal activity, pH 9: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 55
-
45°C: maximal activity, 55°C: drastically reduced activity above, probably because of inactivation of the enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMDA_BORBO
240
0
24735
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24740
electrospray ion mass spectrometry
25940
freshly purified AMDase
25950
calculated molecular mass, including the C-terminal His-tag
26030
crystals of AMDase can only be obtained after storage of the protein stock solution for about 4-5 weeks at 277 K. Electron spray ionization mass spectrometry measurement of a crystallizable AMDase sample shows two main components: 26025 (32%) and 26101 Da (68%), which are 83 and 159 Da higher than that of freshly purified AMDase (25942 Da)
26100
crystals of AMDase can only be obtained after storage of the protein stock solution for about 4-5 weeks at 277 K. Electron spray ionization mass spectrometry measurement of a crystallizable AMDase sample shows two main components: 26025 (32%) and 26101 Da (68%), which are 83 and 159 Da higher than that of freshly purified AMDase (25942 Da)
22000
-
gel filtration
24000
-
1 * 24000, SDS-PAGE
24734
-
1 * 24734, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
G74C/C188S mutant in the liganded form at a resolution of 1.45 A, hanging drop vapor diffusion method, using 1.2 M ammonium sulfate, 15% (w/v) PEG5000, 10 mM bromophenylacetate, 1% (v/v) dioxane, and 70 mM HEPES (pH 7.6)
hanging-drop vapour-diffusion method, crystallized with ammonium sulfate under alkaline pH conditions with the aim of understanding the mechanism of the enantioselective reaction
vapour-diffusion hanging-drop setup
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C188S
G190A
the mutant shows 4.6% relative activity compared to the wild type enzyme
G190S/P14V/P15G
the mutant shows 1.9% relative activity compared to the wild type enzyme
G74C/C188G
the mutant has a 5.6fold increase in activity compared with the G74C/C188S mutant
G74C/C188S
G74C/M159L
the mutant shows 14% decarboxylation activity and 165% racemisation activity compared to mutant G74C
G74C/M159L/C188G
the mutant shows a 210fold increase in activity compared with the G74C/C188S mutant
G74C/M159L/C188G/P14V/P15G
inactive
G74C/M159L/C188G/V43I/A125P/V156l
G74C/V13D/G190H
inactive
G74C/V43A
the mutant with shows a 20fold shift towards promiscuous racemisation based on a reduced activity in the decarboxylation reaction and a 2fold increase in the racemisation activity. The mutant shows an extended substrate range, with a 30fold increase in the reaction rate towards ketoprofen
M159C
the mutant shows 1.4% relative activity compared to the wild type enzyme using phenylmalonate or methyl(phenyl)propanedioic acid as substrate, the mutant shows 1.7% relative activity compared to the wild type enzyme using 2-hydroxy-2-phenylmalonic acid as substrate
M159G
the mutant shows 19% relative activity compared to the wild type enzyme
M159S
the mutant shows 2.6% relative activity compared to the wild type enzyme
M159V
P14V/P15G
Y48F/G74C/C188G
the mutant shows a 23fold increase in activity compared with the G74C/C188S mutant
Y48F/G74C/M159L/C188G
the mutant shows a 920fold activity increase relative to the G74C/C188S mutant
A68C/C188S
-
no specific activity using phenylmalonate as a substrate
C101S
-
mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser. CD spectra indicate that the conformational differences of Cys101Ser and Cys188Ser compared to that of the native enzyme are not significant. Only Cys188Ser shows a drastic decrease in enzyme activity, indicating that Cys188 is located at the active centre
C148S
-
mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser. CD spectra indicate that the conformational differences of Cys101Ser and Cys188Ser compared to that of the native enzyme are not significant. Only Cys188Ser shows a drastic decrease in enzyme activity, indicating that Cys188 is located at the active centre
C171S
-
mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser. CD spectra indicate that the conformational differences of Cys101Ser and Cys188Ser compared to that of the native enzyme are not significant. Only Cys188Ser shows a drastic decrease in enzyme activity, indicating that Cys188 is located at the active centre
C188S
G74C/C188S
G74C/S36N/G74C/C188S
-
enhanced activity compared to G74C/C188S
L72C/C188S
-
no specific activity using phenylmalonate as a substrate
L77C/C188S
-
no specific activity using phenylmalonate as a substrate
M159V
the mutant has no activity with hydroxy(phenyl)propanedioic acid compared to the wild type enzyme
M73C/C188S
-
no specific activity using phenylmalonate as a substrate
P14V/P15G
the mutant has no activity with hydroxy(phenyl)propanedioic acid compared to the wild type enzyme
S36N
-
activity is about 1/10 compared to that of the wild-type enzyme
S36N/G74C/C188S
S71C/C188S
-
mutant exhibits decarboxylation activity and gives the opposite enantiomer to that formed by the wild type enzyme
S76C/C188S
-
no specific activity using phenylmalonate as a substrate
T75C/C188S
-
no specific activity using phenylmalonate as a substrate
V69C/C188S
-
no specific activity using phenylmalonate as a substrate
V70C/C188S
-
no specific activity using phenylmalonate as a substrate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
30°C, 30 min, about 60% loss of activity
4830
6.5 - 8.5
-
4°C, stable for over 6 months
4830
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
below, 10 min, stable
40
-
10 min, about 10% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 6.5-8.5, stable for over 6 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity chromatography
Ni-Sepharose column chromatography, gel filtration
DEAE-Toyopearl column chromatography and Butyl-Toyopearl column chromatography
-
diethylamino ethanol-Toyopearl column chromatography and Butyl-Toyopearl column chromatography
-
mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser
-
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and overexpressed in Escherichia coli
complete gene is cloned into pBAD His A vector, and Escherichia coli Top10 cells are transformed
expressed in Escherichia coli
expressed in Escherichia coli Top10 cells
expression in Escherichia coli
overexpressed in Escherichia coli strain DH5alpha-MCR
expressed in Escherichia coli
-
expressed in Escherichia coli JM109 cells
-
expressed in Escherichia coli strain JM109
-
expression in Escherichia coli
-
mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
enzyme is of biotechnological interest for its use in the synthesis of fine chemicals
synthesis
by immobilization on an amino C2 acrylate carrier the operational stability of the (S)-selective AMDase variant G74C/M159L/C188G/V43I/A125P/V156L is 158fold increased to a half-life of about 8.6 days. Further optimization is achieved by simple immobilization of the cell lysate
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miyamoto, K.; Ohta, H.
Purification and properties of a novel acylmalonate decarboxylase from Alcaligenes bronchisepticus KU 1201
Eur. J. Biochem.
210
475-481
1992
Bordetella bronchiseptica, Bordetella bronchiseptica KU 1201
Manually annotated by BRENDA team
Miyamoto, K.; Ohta, H.
Cloning and heterologous expression of a novel arylmalonate decarboxylase gene from Alcaligenes bronchisepticus KU 1201
Appl. Microbiol. Biotechnol.
38
234-248
1992
Bordetella bronchiseptica, Bordetella bronchiseptica KU 1201
Manually annotated by BRENDA team
Miyazaki, M.; Kakidani, H.; Hanzawa, S.; Ohta, H.
Cysteine 188 revealed as being critical for the enzyme acticity of arylmalonate decarboxylase by site-directed mutagenesis
Biol. Chem. Soc. Jpn.
70
2765-2769
1997
Bordetella bronchiseptica
-
Manually annotated by BRENDA team
Kawasaki, T.; Saito, K.; Ohta, H.
The mode of substrate-recognition mechanism of arylmalonate decarboxylase
Chem. Lett.
4
351-352
1997
Bordetella bronchiseptica
-
Manually annotated by BRENDA team
Fukuyama, Y.; Matoishi, K.; Iwasaki, M.; Takizawa, E.; Miyazaki, M.; Ohta, H.; Hanzawa, S.; Kakidani, H.; Sugai, T.
Preparative-scale Enzyme-catalyzed Synthesis of (R)-?-Fluorophenylacetic Acid.
Biosci. Biotechnol. Biochem.
63
1664-1666
1999
Bordetella bronchiseptica
Manually annotated by BRENDA team
Terao, Y.; Ijima, Y.; Kakidani, H.; Ohta, H.
Enzymatic synthesis of (R)-flurbiprofen
Bull. Chem. Soc. JPN
76
2395-2397
2003
Bordetella bronchiseptica
-
Manually annotated by BRENDA team
Matoishi, K.; Kakidani, H.; Suzuki, M.; Sugai, T.; Ohta, H.; Hanzawa, S.
The first synthesis of both enantiomers of [alpha-2H]phenylacetic acid in high enantiomeric excess
Chem. Commun. (Camb.)
2000
1519-1520
2000
Bordetella bronchiseptica
-
Manually annotated by BRENDA team
Ijima, Y.; Matoishi, K.; Terao, Y.; Doi, N.; Yanagawa, H.; Ohta, H.
Inversion of enantioselectivity of asymmetric biocatalytic decarboxylation by site-directed mutagenesis based on the reaction mechanism
Chem. Commun. (Camb.)
2005
877-879
2005
Bordetella bronchiseptica
Manually annotated by BRENDA team
Matoishi, K.; Ueda, M.; Miyamoto, K.; Ohta, H.
Mechanism of asymmetric decarboxylation of alpha-aryl-alpha-methylmalonate catalyzed by arylmalonate decarboxylase originated from Alcaligenes bronchisepticus
J. Mol. Catal. B
27
161-168
2004
Bordetella bronchiseptica (Q05115), Bordetella bronchiseptica KU 1201 (Q05115)
-
Manually annotated by BRENDA team
Terao, Y.; Miyamoto, K.; Ohta, H.
Improvement of the activity of arylmalonate decarboxylase by random mutagenesis
Appl. Microbiol. Biotechnol.
73
647-653
2006
Bordetella bronchiseptica
Manually annotated by BRENDA team
Terao, Y.; Miyamoto, K.; Ohta, H.
Introduction of single mutation changes arylmalonate decarboxylase to racemase
Chem. Commun. (Camb. )
34
3600-3602
2006
Bordetella bronchiseptica, Bordetella bronchiseptica KU1201
Manually annotated by BRENDA team
Terao, Y.; Miyamoto, K.; Ohta, H.
The aldol type reaction catalyzed by arylmalonate decarboxylase - a decarboxylase can catalyze an entirely different reaction, aldol reaction -
Chem. Lett.
36
420-421
2007
Bordetella bronchiseptica, Bordetella bronchiseptica KU1201
-
Manually annotated by BRENDA team
Miyamoto, K.; Tsutsumi, T.; Terao, Y.; Ohta, H.
Stereochemistry of decarboxylation of arylmalonate catalyzed by mutant enzymes
Chem. Lett.
36
656-657
2007
Bordetella bronchiseptica
-
Manually annotated by BRENDA team
Terao, Y.; Ijima, Y.; Miyamoto, K.; Ohta, H.
Inversion of enantioselectivity of arylmalonate decarboxylase via site-directed mutation based on the proposed reaction mechanism
J. Mol. Catal. B
45
15-20
2007
Bordetella bronchiseptica, Bordetella bronchiseptica KU1201
-
Manually annotated by BRENDA team
Nakasako, M.; Obata, R.; Okubo, R.; Nakayama, S.; Miyamoto, K.; Ohta, H.
Crystallization and preliminary X-ray diffraction experiments of arylmalonate decarboxylase from Alcaligenes bronchisepticus
Acta Crystallogr. Sect. F
64
610-613
2008
Bordetella bronchiseptica (Q05115), Bordetella bronchiseptica, Bordetella bronchiseptica KU1201 (Q05115)
Manually annotated by BRENDA team
Tamura, K.; Terao, Y.; Miyamoto, K.; Ohta, H.
Asymmetric decarboxylation of alpha -hydroxy- and alpha -amino-alpha -phenylmalonate catalyzed by arylmalonate decarboxylase from Alcaligenes bronchisepticus
Biocatal. Biotransform.
26
253-257
2008
Bordetella bronchiseptica (Q05115), Bordetella bronchiseptica KU 1201 (Q05115)
-
Manually annotated by BRENDA team
Okrasa, K.; Levy, C.; Hauer, B.; Baudendistel, N.; Leys, D.; Micklefield, J.
Structure and mechanism of an unusual malonate decarboxylase and related racemases
Chem. Eur. J.
14
6609-6613
2008
Alkaliphilus metalliredigens QYMF, Bordetella bronchiseptica (A0A0H3LJU9), Bordetella bronchiseptica (Q05115), Bordetella bronchiseptica KU1201 (Q05115), Bordetella bronchiseptica RB50 (A0A0H3LJU9), Chelativorans sp. BNC1, Pyrococcus horikoshii (O58713), Pyrococcus horikoshii OT-3 (O58713)
Manually annotated by BRENDA team
Kuettner, E.B.; Keim, A.; Kircher, M.; Rosmus, S.; Straeter, N.
Active-site mobility revealed by the crystal structure of arylmalonate decarboxylase from Bordetella bronchiseptica
J. Mol. Biol.
377
386-394
2008
Bordetella bronchiseptica (Q05115), Bordetella bronchiseptica
Manually annotated by BRENDA team
Okrasa, K.; Levy, C.; Wilding, M.; Goodall, M.; Baudendistel, N.; Hauer, B.; Leys, D.; Micklefield, J.
Structure-guided directed evolution of alkenyl and arylmalonate decarboxylases
Angew. Chem. Int. Ed. Engl.
48
7691-7694
2009
Bordetella bronchiseptica (Q05115)
Manually annotated by BRENDA team
Obata, R.; Nakasako, M.
Structural basis for inverting the enantioselectivity of arylmalonate decarboxylase revealed by the structural analysis of the Gly74Cys/Cys188Ser mutant in the liganded form
Biochemistry
49
1963-1969
2010
Bordetella bronchiseptica (Q05115)
Manually annotated by BRENDA team
Wong, L.S.; Okrasa, K.; Micklefield, J.
Site-selective immobilisation of functional enzymes on to polystyrene nanoparticles
Org. Biomol. Chem.
8
782-787
2010
Bordetella bronchiseptica
Manually annotated by BRENDA team
Miyauchi, Y.; Kourist, R.; Uemura, D.; Miyamoto, K.
Dramatically improved catalytic activity of an artificial (S)-selective arylmalonate decarboxylase by structure-guided directed evolution
Chem. Commun. (Camb. )
47
7503-7505
2011
Bordetella bronchiseptica (Q05115)
Manually annotated by BRENDA team
Kourist, R.; Miyauchi, Y.; Uemura, D.; Miyamoto, K.
Engineering the promiscuous racemase activity of an arylmalonate decarboxylase
Chemistry
17
557-563
2011
Bordetella bronchiseptica (Q05115)
Manually annotated by BRENDA team
Lind, M.; Himo, F.
Theoretical study of reaction mechanism and stereoselectivity of arylmalonate decarboxylase
ACS Catal.
4
4153-4160
2014
Bordetella bronchiseptica (Q05115)
-
Manually annotated by BRENDA team
Gassmeyer, S.; Wetzig, J.; Mgge, C.; Assmann, M.; Enoki, J.; Hilterhaus, L.; Zuhse, R.; Miyamoto, K.; Liese, A.; Kourist, R.
Arylmalonate decarboxylase-catalyzed asymmetric synthesis of both enantiomers of optically pure flurbiprofen
ChemCatChem
8
916-921
2016
Bordetella bronchiseptica (Q05115)
-
Manually annotated by BRENDA team
Lewin, R.; Goodall, M.; Thompson, M.L.; Leigh, J.; Breuer, M.; Baldenius, K.; Micklefield, J.
Enzymatic enantioselective decarboxylative protonation of heteroaryl malonates
Chemistry
21
6557-6563
2015
Bordetella bronchiseptica, Bordetella bronchiseptica (Q05115)
Manually annotated by BRENDA team
Assmann, M.; Muegge, C.; Gassmeyer, S.K.; Enoki, J.; Hilterhaus, L.; Kourist, R.; Liese, A.; Kara, S.
Improvement of the process stability of arylmalonate decarboxylase by immobilization for biocatalytic profen synthesis
Front. Microbiol.
8
448
2017
Bordetella bronchiseptica (Q05115)
Manually annotated by BRENDA team