Information on EC 4.1.1.12 - aspartate 4-decarboxylase

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

EC NUMBER
COMMENTARY hide
4.1.1.12
-
RECOMMENDED NAME
GeneOntology No.
aspartate 4-decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartate = L-alanine + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
desulfination
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
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Cysteine and methionine metabolism
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Metabolic pathways
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alanine metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate 4-carboxy-lyase (L-alanine-forming)
A pyridoxal-phosphate protein. Also catalyses the decarboxylation of aminomalonate (formerly listed as EC 4.1.1.10), and the desulfination of 3-sulfino-L-alanine to sulfite and alanine.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-57-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain CCRC 11585
SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Pseudomonas dacunhae
Pseudomycobacteria
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Aminomalonate
Gly + CO2
show the reaction diagram
beta-chloro-L-Ala + H2O
pyruvate + Cl- + NH4+
show the reaction diagram
-
-
-
-
erythro-beta-hydroxy-DL-Asp
?
show the reaction diagram
Pseudomonas dacunhae
-
the reaction of erythro-beta-hydroxy-DL-Asp with ABDC is at least 16700fold slower than that with L-aspartate
-
-
?
erythro-beta-Hydroxyaspartate
L-Ser + CO2
show the reaction diagram
-
-
-
-
L-Asp
?
show the reaction diagram
-
in coordination with pyruvate carboxylase, aspartate 4-decarboxylase is important in regulating the metabolic fate of oxaloacetate and thus plays a role in determining the efficiency of carbohydrate metabolism
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-
-
L-Asp
L-Ala + CO2
show the reaction diagram
L-aspartate
beta-alanine + CO2
show the reaction diagram
-
more than 95% of the substrate is converted to beta-alanine during a 20 min incubation period
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-
?
L-aspartate
L-alanine + CO2
show the reaction diagram
L-aspartic acid
L-alanine + CO2
show the reaction diagram
Pseudomonas dacunhae
-
-
-
-
-
L-Cysteinesulfinate
L-Ala + SO2
show the reaction diagram
succinate
?
show the reaction diagram
Pseudomonas dacunhae
-
-
-
-
?
threo-beta-hydroxy-DL-Asp
?
show the reaction diagram
Pseudomonas dacunhae
-
the reaction of threo-beta-hydroxy-DL-Asp with ABDC is at least 1000fold slower than that with L-aspartate
-
-
?
threo-beta-Hydroxyaspartate
L-Ser + CO2
show the reaction diagram
-
-
-
-
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
L-Asp
?
show the reaction diagram
-
in coordination with pyruvate carboxylase, aspartate 4-decarboxylase is important in regulating the metabolic fate of oxaloacetate and thus plays a role in determining the efficiency of carbohydrate metabolism
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-
-
L-aspartate
L-alanine + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no divalent metal ion required for catalysis
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
-
-
Ala
-
liver enzyme
aminomalonate
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decarboxylation is accompanied by a slower reaction in which the enzyne becomes irreversibly inactivated, and in which aminomalonate becomes tightly bound to the enzyme
Aminooxyacetate
-
-
beta-Ala
beta-chloro-L-Ala
-
reacts with a specific glutamic acid residue at the active center of the enzyme
Ca2+
-
10 mM, 14% inhibition
Co2+
-
10 mM, over 90% inhibition
Cys
-
liver enzyme
DL-beta-Methylaspartate
-
-
DL-erythro-beta-hydroxyaspartate
-
-
DL-threo-beta-hydroxyaspartate
-
-
Fe2+
-
10 mM, over 90% inhibition
fumarate
Pseudomonas dacunhae
-
-
Gln
-
liver enzyme
Glu
-
liver enzyme
Hg2+
-
10 mM, complete inhibition
hydroxylamine
-
-
iodoacetate
L-cysteine sulfinate
Pseudomonas dacunhae
-
-
malate
Pseudomonas dacunhae
-
-
Maleate
malonate
Pseudomonas dacunhae
-
-
Mg2+
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10 mM, 64% inhibition
Mn2+
-
10 mM, over 90% inhibition
Ni2+
-
10 mM, over 90% inhibition
phosphate
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strong inhibition by phosphate buffers above pH 5.0
potassium borohydride
-
-
Ser
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activates liver enzyme, competitively inhibits kidney and brain enzyme
succinate
Tartrate
Val
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weak, liver enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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1 mM, 7% activation
2-Oxo-5-carbamidopentanoate
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activates
2-oxo-5-guanidinopentanoate
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activates
2-oxoglutarate
2-Oxoisohexanoate
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activates
2-oxoisopentanoate
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activates
2-Oxomalonate
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activates
2-oxophenylacetate
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activates
acetaldehyde
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activates
beta-cyano-L-Ala
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competitive towards L-Asp
D-2-Oxo-3-methylpentanoate
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activates
DL-erythro-3-hydroxyaspartate
Pseudomonas dacunhae
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-
DL-threo-3-hydroxyaspartate
Pseudomonas dacunhae
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-
DTT
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1 mM, 7% activation
EDTA
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10-20 mM, 10% activation
glutamate
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stimulates
Glyoxal
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activates
glyoxylate
L-2-Oxo-3-methylpentanoate
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activates
oxalacetate
phenylpyruvate
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activates
pyruvate
Ser
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acticates liver enzyme, competitively inhibits kidney and brain enzyme
additional information
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interacts with a number of vitamin B6 5'-phosphate analogues
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
aminomalonate
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-
0.063
beta-chloro-L-Ala
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-
0.024
erythro-beta-hydroxyaspartate
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0.08 - 150
L-Asp
0.22 - 11.5
L-aspartate
4.8
L-cysteinesulfinate
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-
0.089
threo-beta-hydroxyaspartate
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-
additional information
additional information
Pseudomonas dacunhae
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 442
L-Asp
0.65
L-aspartate
Mycobacterium tuberculosis
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37°C, pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
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mutant enzyme P257H, in acetate buffer (pH 5.0) at 40°C; mutant enzyme S298R, in acetate buffer (pH 5.0) at 40°C; mutant enzyme Y207H, in acetate buffer (pH 5.0) at 40°C
0.06
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recombinant wild-type enzyme, aminotransferase activity
0.084
Pseudomonas dacunhae
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20.3
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wild type enzyme, in acetate buffer (pH 5.0) at 40°C
75.45
35°C, pH 6.8
128.8
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recombinant wild-type enzyme, 4-decarboxylation activity
280
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purified recombinant enzyme, pH 5.0, 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5
Pseudomonas dacunhae
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transamination between Asp and 2-oxoglutarate
3.5 - 6
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4
Pseudomonas dacunhae
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cysteine sulfinate desulfinase activity
5.3
Pseudomonas dacunhae
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aspartate decarboxylase activity
6.2
Pseudomonas dacunhae
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7.1 - 7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 5
Pseudomonas dacunhae
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pH 3: about 35% of maximal activity, pH 5: about 40% of maximal activity, cysteine sulfinate desulfinase activity
4 - 6
Pseudomonas dacunhae
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about 20% of maximal activity at pH 4 and pH 6, aspartate decarboxylase activity
5.7 - 8.1
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about 60% of maximal activity at pH 5.7 and pH 8.1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
Pseudomonas dacunhae
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cysteine sulfinate desulfinase activity
45 - 55
47
Pseudomonas dacunhae
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decarboxylation and transamination
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 55
approx. 25% of maximal activity at 55°C and 20°C
20 - 40
Pseudomonas dacunhae
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20°C: about 60% of maximal activity, 40°C: about 20% of maximal activity, cysteine sulfinate desulfinase activity
30 - 50
40 - 45
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92% of maximal activity at 40°C, maximal activity at 45°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
predicted from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
highest activity in the cortex, lowest activity in the striatum and hippocampus
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas dacunhae ATCC 21192
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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4 * 16000, SDS-PAGE, PanD is expressed as 16000 Da pro-protein that is processed into 1 alpha and 1 beta subunit
59243
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12 * 63000, pH 7.0, SDS-PAGE, 12 * 59243, sequence calculation; 2 * 63000, pH 7.0, SDS-PAGE, 2 * 59243, sequence calculation
59580
x * 59580, deduced from nucleotide sequence
61000
x * 61000, SDS-PAGE
63000
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12 * 63000, pH 7.0, SDS-PAGE, 12 * 59243, sequence calculation; 2 * 63000, pH 7.0, SDS-PAGE, 2 * 59243, sequence calculation
64000
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gel filtration
110000
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gel filtration
760000
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dodedamer, pH 5.0, recombinant enzyme, gel filtration
795000
Pseudomonas dacunhae
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calculation from sedimentation and diffusion data
820000
Pseudomonas dacunhae
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low speed sedimenation without reaching equilibrium
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 59580, deduced from nucleotide sequence; x * 61000, SDS-PAGE
dodecamer
homododecamer
tetramer
additional information
Pseudomonas dacunhae
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enzyme exists in a 16-subunit associated state in dilute solutions
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 15% (w/v) PEG4000 and 0.1 M lithium sulfate in 0.1 M Tris-HCl buffer (pH 7.4-8.5)
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Pseudomonas dacunhae
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microbatch-under-oil method, using 100 mM MgCl2, 100 mM Tris, pH 8.5, 25% (v/v) polyethylene glycol (PEG) 400, and 10% (v/v) glycerol
Pseudomonas dacunhae
hanging drop vapor diffusion method, using 40% (w/v) PEG400 and 0.1 M lithium sulfate in 0.1 M Tris-HCl buffer (pH 8.4)
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8.5
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purified recombinant enzyme, 4°C, 1 day, completely stable
677736
5
-
rapid loss of activity
3951
6
-
irreversible inactivation below
3962
7
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4°C, stable in concentrated solution
3951
10
-
stable up to
3962
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
Pseudomonas dacunhae
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half life of activity in immobilized cells: 100 days
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rapid loss of activity in dilute solution
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when immobilized cells are treated with 0.4 M glutaraldehyde in presence of 0.4-0.5 M L-Lys, a very stable immobilized preparation is obtained
Pseudomonas dacunhae
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, 0.05 M acetate buffer, pH 5.2, 52% loss of activity after 6 days, complete loss of activity after 16 days
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-15°C, 0.05 M acetate buffer, pH 5.2, 59% loss of activity after 6 days, complete loss of activity after 12 days
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4°C, 0.05 M acetate buffer, pH 5.2, rapid loss of activity
4°C, pH 7, stable in concentrated solution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Sepharose CL-6B resin gel filtration
Pseudomonas dacunhae
chitin bead column chromatography, Mono-Q column chromatography, hydroxylapatite column chromatography, and gel filtration
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HiTrap chelating column chromatography
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Ni-NTA column chromatography and HPLC gel filtration
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant panD
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
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expression Escherichia coli
expression in Escherichia coli
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gene asd, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of the C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene asd, DNA and amino acid sequence determination and analysis, sequence comparisons
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ENGINEERING
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
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K315A
-
the mutant shows 36.7% activity compared to the wild type enzyme
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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)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
-
Asd is a major enzyme used in the industrial production of L-alanine
synthesis