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4.1.1.11: aspartate 1-decarboxylase

This is an abbreviated version!
For detailed information about aspartate 1-decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.11

Reaction

L-aspartate
=
beta-Alanine
+
CO2

Synonyms

ACD, ADC, ADCBs, ADCC.g, ADCCg, ADCE, Aspartate alpha-decarboxylase, aspartate decarboxylase, aspartate-alpha-decarboxylase, Aspartic alpha-decarboxylase, AspDC, BmADC, BsADC, CgADC, Dgad2, GcADC, L-Aspartate alpha-decarboxylase, L-Aspartate-alpha-decarboxylase, MfnA, MJ0050, More, MtbADC, PanD, PF1159, PLP-dependent L-aspartate decarboxylase, pyruvoyl-dependent l-aspartate alpha-decarboxylase, TK1814

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.11 aspartate 1-decarboxylase

Engineering

Engineering on EC 4.1.1.11 - aspartate 1-decarboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q377L
-
site-directed mutagenesis, mutation at position 377 from glutamine to leucine in aspartate 1-decarboxylase diminishes its decarboxylation activity to aspartate with no major effect on its cysteine sulfinic acid decarboxylase activity
D41G
site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type
E56S
site-directed mutagenesis, the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production, but no significant effect on the cell growth properties or the molecular weight of BsADC. The E56S mutant shows a 1.6fold higher activity and an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuates the mechanism-based inactivation of the enzyme. The mutant enzyme catalyzes the beta-alanine synthesis with a very high product yield of 215.3 g per liter culture. In BsADC, Glu56 corresponds to Ser56 in the center channel of the homotetramer ADC from Escherichia coli. Due to the shorter side chain of Ser56, the Glu56-to-Ser56 mutation may enhance the import of the Asp substrate and export of the beta-alanine product in the tetramer channel
I188M
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type
K63E
site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type
D41G
-
site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type
-
E56S
-
site-directed mutagenesis, the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production, but no significant effect on the cell growth properties or the molecular weight of BsADC. The E56S mutant shows a 1.6fold higher activity and an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuates the mechanism-based inactivation of the enzyme. The mutant enzyme catalyzes the beta-alanine synthesis with a very high product yield of 215.3 g per liter culture. In BsADC, Glu56 corresponds to Ser56 in the center channel of the homotetramer ADC from Escherichia coli. Due to the shorter side chain of Ser56, the Glu56-to-Ser56 mutation may enhance the import of the Asp substrate and export of the beta-alanine product in the tetramer channel
-
I188M
-
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type
-
K63E
-
site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type
-
R3A
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3D
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3E
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3L
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3N
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3Q
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R54A
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
R54K
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
Y58A
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
Y58T
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
R3A
-
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
-
R3Q
-
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
-
R54A
-
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
-
R54K
-
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
-
Y58A
-
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
-
G24S
study of the structure and processing activity
H11A
study of the structure and processing activity
I60A
site-directed mutagenesis, the PanD activation activity is affected
I86A
site-directed mutagenesis, the PanD activation activity is affected
K115A
-
site-directed mutagenesis, the mutation is introduced in vitro by overlap extension PCR
K119A
-
site-directed mutagenesis, the mutation is introduced in vitro by overlap extension PCR. Complex formation of the site-directed mutants PanZ(R73A) and PanD(K119A) leads to a complex that still complements the beta-alanine auxotrophy of the DELTApanZ and DELTApanD strains, indicating that catalytically active PanD is formed, but no growth inhibition is observed as a result of PanZ overexpression
K14A
-
site-directed mutagenesis, the mutation is introduced in vitro by overlap extension PCR
K53A
-
site-directed mutagenesis, the mutation is introduced in vitro by overlap extension PCR
N72A
site-directed mutagenesis, in the Asn72Ala mutant the C-terminal region residues are ordered, in contrast to the wild-type enzyme, owing to an interaction with the active site of the neighbouring symmetry-related multimer
S25A
inactive mutant, study of the structure and processing activity
S25C
study of the structure and processing activity
S25T
inactive mutant, study of the structure and processing activity
S70A
site-directed mutagenesis, the PanD activation activity is affected
W47A
site-directed mutagenesis, the PanD activation activity is affected
Y22F
site-directed mutagenesis, the PanD activation activity is affected
Y58F
site-directed mutagenesis, the PanD activation activity is affected
A128E
-
naturally occuring mutation after treatment with pyrazinoic acid
A128S
-
naturally occuring mutation after treatment with pyrazinoic acid
C17R
-
naturally occuring mutation after treatment with pyrazinoic acid
D116Y
-
naturally occuring mutation after treatment with pyrazinoic acid
E130G
-
naturally occuring mutation after treatment with pyrazinoic acid
F107L
-
naturally occuring mutation after treatment with pyrazinoic acid
H21N
-
naturally occuring mutation after treatment with pyrazinoic acid
H21Q
-
naturally occuring mutation after treatment with pyrazinoic acid
I115V
-
naturally occuring mutation after treatment with pyrazinoic acid
L131P
-
naturally occuring mutation after treatment with pyrazinoic acid
L136P
-
naturally occuring mutation after treatment with pyrazinoic acid
L136R
-
naturally occuring mutation after treatment with pyrazinoic acid
M117I
-
naturally occuring mutation after treatment with pyrazinoic acid
M117V
-
naturally occuring mutation after treatment with pyrazinoic acid
N127K
-
naturally occuring mutation after treatment with pyrazinoic acid
V138A
-
naturally occuring mutation after treatment with pyrazinoic acid
V138M
-
naturally occuring mutation after treatment with pyrazinoic acid
additional information