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4.1.1.12: aspartate 4-decarboxylase

This is an abbreviated version!
For detailed information about aspartate 4-decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.12

Reaction

L-aspartate
=
L-alanine
 +
CO2

Synonyms

ABDC, ADC, Aminomalonic decarboxylase, Asd, aspartate 4-carboxylyase, Aspartate beta-decarboxylase, Aspartate omega-decarboxylase, aspartate-beta-decarboxylase, Aspartic beta-decarboxylase, Aspartic omega-decarboxylase, Cysteine sulfinic desulfinase, Decarboxylase, aspartate 4-, Desulfinase, EC 4.1.1.10, L-Asparate 4-carboxy-lyase, L-aspartate 4-decarboxylase, L-Aspartate beta-decarboxylase, L-Cysteine sulfinate acid desulfinase, PanD

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.12 aspartate 4-decarboxylase

Engineering

Engineering on EC 4.1.1.12 - aspartate 4-decarboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E84K/E88K
the mutant retains 13% activity compared to the wild type enzyme
K17A
the mutant shows 131.2% activity compared to the wild type enzyme
K315A
the mutant shows 36.7% activity compared to the wild type enzyme
R37A
the mutant shows 10.4% activity compared to the wild type enzyme
R425A
the mutant retains 2.5% activity compared to the wild type enzyme
R487A
completely inactive mutant
S67A/Y68A/M69A
the mutant retains less than 1% activity compared to the wild type enzyme
S67E/Y68E/M69E
the mutations produce an inactive dimer
S67R/Y68R/M69R
the mutations produce an inactive dimer
Y134F
the mutant shows 40.3% activity compared to the wild type enzyme
Y207F
the mutant shows 10.7% activity compared to the wild type enzyme
Y441F
the mutant shows 40.8% activity compared to the wild type enzyme
K17A
-
the mutant shows 131.2% activity compared to the wild type enzyme
-
K315A
-
the mutant shows 36.7% activity compared to the wild type enzyme
-
R37A
-
the mutant shows 10.4% activity compared to the wild type enzyme
-
R425A
-
the mutant retains 2.5% activity compared to the wild type enzyme
-
R487A
-
completely inactive mutant
-
S298R
Pseudomonas dacunhae
the mutant shows very low activity
D360P
site-directed mutagenesis, the mutant shows similar 4-decarboxylation activity but reduced aminotransferase compared to the wild-type enzyme
F204W
site-directed mutagenesis, the mutant shows slightly reduced 4-decarboxylation activity but highly increased aminotransferase compared to the wild-type enzyme
H123Y
site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity and slightly increased aminotransferase compared to the wild-type enzyme
H337R
site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity but similar aminotransferase compared to the wild-type enzyme
K347R
site-directed mutagenesis, the mutant shows similar 4-decarboxylation activity but reduced aminotransferase compared to the wild-type enzyme
M178L
site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity but unaltered aminotransferase compared to the wild-type enzyme
P257H
-
the mutation results in inactivation of the enzyme, but does not affect the overall structure (0.08% of the wild type enzymatic activity)
S298R
-
the mutation disassembles the dodecameric L-aspartate 4-decarboxylase into inactive dimers (0.1% of the wild type enzymatic activity)
V475L
site-directed mutagenesis, the mutant shows slightly reduced 4-decarboxylation activity but unaltered aminotransferase compared to the wild-type enzyme
Y207H
-
the mutation results in inactivation of the enzyme, but does not affect the overall structure (0.08% of the wild type enzymatic activity)