Information on EC 4.1.1.11 - aspartate 1-decarboxylase

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

EC NUMBER
COMMENTARY hide
4.1.1.11
-
RECOMMENDED NAME
GeneOntology No.
aspartate 1-decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartate = beta-alanine + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
beta-alanine biosynthesis III
-
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beta-Alanine metabolism
-
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Biosynthesis of secondary metabolites
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Metabolic pathways
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Pantothenate and CoA biosynthesis
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alanine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate 1-carboxy-lyase (beta-alanine-forming)
The Escherichia coli enzyme contains a pyruvoyl group.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-58-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
strain 26695
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Manually annotated by BRENDA team
strain H37Rv
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Manually annotated by BRENDA team
serovar Typhimurium LT2, gene panD
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Manually annotated by BRENDA team
strain GA-1, red flour beetle
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
ADC suppression favors formation of melanic pigment with a decrease in protein cross-linking
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Aspartate
beta-Ala + CO2
show the reaction diagram
L-aspartate
beta-alanine + CO2
show the reaction diagram
L-aspartic acid
beta-alanine + CO2
show the reaction diagram
additional information
?
-
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-aspartate
beta-alanine + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyruvoyl cofactor
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S,3R,4S,5S)-2,3,4,6-tetrahydroxy-5-mercaptohexanal
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ZINC03871163
(2S,3S,4R,5R)tetrahydro-2H-pyran2,3,4,5-tetraol
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ZINC03606295
(2S,3S,4R,5S)2,5bis(hydroxymethyl)tetrahydrofuran-2,3,4-triol
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ZINC03830875
(2S,3S,4S,5R)-2(hydroxymethyl) tetrahydro-2H-pyran-2,3,4,5-tetraol
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ZINC03830878
(S)-5-acetoxy-4-methylpentanoate
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ZINC02036492
(S)-thiazolidin-3-ium-4-carboxylate
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ZINC00967474
1H-pyrazolo[3,4-d]pyrimidin-4(7H)-one
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ZINC05177572
2,4-dihydroxypyrimidine-5-carboxylate
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ZINC00901606, moderate inhibition
2-(difluoromethyl)-L-aspartic acid
3-amino-4-(propylamino)cyclobutane-1 2-dione
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LIGAND10436
beta-hydroxy-DL-Asp
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CuCl
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10 mM, 88% inhibition
D-tagatose
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ZINC03830878, weak inhibition
D-Tartrate
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ZINC00895296, strong inhibition
DL-threo-beta-hydroxyaspartate
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strong inhibition
hydroxylamine
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KCl
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200 mM, 63% inhibition
L-aspartate
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substrate inhibition
L-cysteic acid
L-glutamate
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strong inhibition
L-serine
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weak inhibition
L-Tartrate
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ZINC00895301, strong inhibition
oxaloacetate
phenylhydrazine
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succinate
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
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acetyl-CoA is required for activation
PanM
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Salmonella enterica PanM, formerly YhhK, a Gcn5-like N-acetyltransferase, is necessary for pro-PanD maturation, both in vitro and in vivo. PanM-dependent pro-PanD maturation does not involve an acetyl transfer event. CoA binding to PanM is needed for in vivo activity, disruption of CoA binding prevents PanM from interacting with PanD. PanM lacks acetyltransferase activity but functions instead as an acetyl-coenzyme A (CoA) sensor, overview
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PanZ
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Pyruvoyl group
YhhK
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or PanM, the protein interacts directly with PanD, such interactions accelerate pro-PanD maturation, analysis by yeast two hybrid system. One PanM monomer (14.5 kDa) interacts with one PanD tetramer (55.6 kDa)
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.151 - 0.16
L-Asp
0.219 - 3.18
L-aspartate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.57
L-Asp
Escherichia coli
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-
0.65 - 7.03
L-aspartate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.66 - 3.44
L-aspartate
97
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.09
pH 8.0, 70C, recombinant enzyme
0.83
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crude recombinant enzyme, pH 6.0, 37C
1.72
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purified recombinant enzyme, pH 6.0, 37C
2.1
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pH 7, 37C, recombinant enzyme
2.4
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self-cleavage activity, purified recombinant mutant Z58A, pH 7.4, 37C
2.6
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self-cleavage activity, purified recombinant mutant Z58T, pH 7.4, 37C
3.5
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self-cleavage activity, purified recombinant mutant R54A, pH 7.4, 37C
4
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self-cleavage activity, purified recombinant mutant R54K, pH 7.4, 37C
690
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self-cleavage activity, purified recombinant wild-type enzyme, pH 7.4, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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recombinant enzyme
6.5 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
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activity range, profile overview
5.3 - 8.6
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half-maximal activity at pH 5.3 and at pH 8.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
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activity range, profile overview
26 - 78
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half-maximal activity at 26C and at 78C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
enzyme expression analysis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11000
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x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine
14100
x * 14100, pi-protein, calculated from the amino acid sequence
16000
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4 * 16000, recombinant enzyme, inactive pi-proenzyme, which is cleaved into the 13.22 kDa alpha-subunit and 2.74 kDa beta-subunit, processing is not essential for tetramer formation, SDS-PAGE
59000
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gel filtration
64000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE
octamer
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two tetramers forming a pseudo fourfold rotational symmetry, the enzyme protein shows a double-psi beta-barrel structure
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.2. A resolution
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crystal structure of an unprocessed native proenzyme and of the mutants G24S, S25A, S25C, S25T, H11A, Ala-24 and Ala-26 insertion mutants, hanging-drop vapour-diffusion method
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purified recombinant mutant N72A, hanging drop vapour diffusion method, mixing of 0.001 ml of 19 mg /ml protein in 50 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 1.6 M ammonium sulfate, pH 4.0, and equilibration against 0.5 ml of reservoir solution, 19C, 3 days, cryoprotection by 1.8 M ammonium sulfate, 0.1 M citric acid, 30% glycerol pH 4.0 using 5% increments in glycerol concentration to prevent crystal dissolution, X-ray diffraction structure determination and analysis at 1.7 A resolution
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purified recombinant T57V mutant enzyme, hanging drops by vapour diffusion with a 1:1 ratio of protein to precipitant, 7.5 mg/ml protein, 1.5-3.4 M sodium malonate, pH 4.0, method optimization, 17C, X-ray diffraction structure determination and analysis at 1.62 A resolution, modeling
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both apo form and in complex with isoasparagine
recombinant enzyme in the presence of the substrate analogue isoasparagine, hanging-drop vapour-diffusion method, X-ray analysis
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purified recombinant His-tagged unprocessed, native precursor ADC, vapor diffusion hanging drop method, the precipitant solution contains 0.1 M sodium cacodylate, pH 6.5, 1.5 M magnesium sulfate, and 20% w/v PEG 2000, 15 days, cryoprotection by 20% v/v glycerol, X-ray diffraction structure determination and analysis at 2.99 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
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purified recombinant enzyme, highly stable at, the enzyme retains over 80% activity within this range after 12 h at 37C
727235
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16 - 37
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purified recombinant enzyme, highly stable at, the enzyme retains over 30% activity within this range after 12 h at pH 6.0, inactivation at 80C and above
additional information
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thermotolerance of transgenic tobacco plants expressing the enzyme, overview
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from Salmonella enterica strain JE13153 lacking panM by anion exchange chromatography
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native pro-ADC and mutants
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recombinant enzyme
recombinant enzyme 2.1fold from Escherichia coli strain BL21(DE3) by anion exchange chromatography and gel filtration
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recombinant enzyme mutant N72A from Escherichia coli strain C41 (DE3) to homogeneity
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration
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recombinant His-tagged enzyme mutant T57V and PanZ from Escherichia coli strain DELTApanD DELTApanZ (DE3) by nickel affinity chromatography and gel filtration
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recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, gel filtration, and dialysis
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recombinant nontagged enzyme in Escherichia coli panZ-deficient strain SN227 by ultrafiltration, ammonium sulfate fractionation, dialysis, and anionexchange chromatography, recombinant His-tagged wild-type and mutant enzymes and flag3-tagged enzyme from Escherichia coli strain MG1655 by affinity chromatography and dialysis
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recombinant wild-type and mutant enzymes from Escherichia coli
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recomnbinant enzyme from strain BL21(DE3) by anion exchange chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADC expression analysis, expression of the HIs-tagged enzyme in Escherichia coli
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expressed in Nicotiana tabacum
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expression of His6tagged enzyme in Escherichia coli
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gene panD, expression of Corynebacterium glutamicum panD in Salmonella enterica panM deficient strain JE13233 shows functional complementation, thus the Corynebacterium glutamicum enzyme does not required panM activation
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gene panD, expression of enzyme mutant N72A in Escherichia coli strain C41 (DE3)
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gene panD, expression of His-tagged enzyme mutant T57V and PanZ in Escherichia coli strain DELTApanD DELTApanZ (DE3)
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gene panD, expression of wild-type and mutant enzymes in Escherichia coli
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gene panD, heterologous expression in panM-deficient Salmonella enterica strain JE13153, functional complementation in PanD activity
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gene panD, phylogenetic tree, expression of nontagged enzyme in Escherichia coli panZ-deficient strain SN227, expression of His-tagged wild-type and mutant enzymes in Escherichia coli, expression of flag3-tagged enzyme from gene panD with the cat gene inserted between frt sites in Escherichia coli strain MG1655
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gene panD, recombinant expression in Escherichia coli strain BL21(DE3)
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gene panD, subcloning and expression in strain DH5alpha, BL21(DE3), and in an enzyme-deficient strain, functional expression under the constitutive CaMV 35S promoter in transgenic Nicotiana tabacum cv. Havana 38 leaves using the Agrobacterium tumefaciens transfection system
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overexpression
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overexpression in Escherichia coli
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panD gene overexpression
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panD gene, overexpression in Corynebacterium glutamicum with 4fold increased enzyme activity and in Escherichia coli with 3fold increased enzyme activity
panD gene, overexpression in Escherichia coli C41(DE3)
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panD gene, overexpression in Escherichia coli, sequencing
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panD gene, sequencing, overexpression in Corynebacterium glutamicum with 288fold increased enzyme activity and in Escherichia coli with 41fold increased enzyme activity
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ADC mRNA is most abundant prior to the pupal-adult molt
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q377L
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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
R3A
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site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3D
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site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3E
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site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3L
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site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3N
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site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3Q
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site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R54A
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site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
R54K
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site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
Y58A
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site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
Y58T
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site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
R3A
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site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
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R3Q
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site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
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R54A
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site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
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R54K
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site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
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Y58A
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site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
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G24S
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study of the structure and processing activity
H11A
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study of the structure and processing activity
I60A
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site-directed mutagenesis, the PanD activation activity is affected
I86A
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site-directed mutagenesis, the PanD activation activity is affected
N72A
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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
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inactive mutant, study of the structure and processing activity
S25C
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study of the structure and processing activity
S25T
-
inactive mutant, study of the structure and processing activity
S70A
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site-directed mutagenesis, the PanD activation activity is affected
W47A
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site-directed mutagenesis, the PanD activation activity is affected
Y22F
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site-directed mutagenesis, the PanD activation activity is affected
Y58F
-
site-directed mutagenesis, the PanD activation activity is affected
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
pharmacology
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