Information on EC 4.1.1.86 - diaminobutyrate decarboxylase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
4.1.1.86
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RECOMMENDED NAME
GeneOntology No.
diaminobutyrate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-2,4-diaminobutanoate = propane-1,3-diamine + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycine, serine and threonine metabolism
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Microbial metabolism in diverse environments
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norspermidine biosynthesis
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polyamine pathway
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rhizobactin 1021 biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
L-2,4-diaminobutanoate carboxy-lyase (propane-1,3-diamine-forming)
A pyridoxal-phosphate protein that requires a divalent cation for activity [1]. N4-Acetyl-L-2,4-diaminobutanoate, 2,3-diaminopropanoate, ornithine and lysine are not substrates. Found in the proteobacteria Haemophilus influenzae and Acinetobacter baumannii. In the latter, this enzyme is cotranscribed with the dat gene that encodes EC 2.6.1.76, diaminobutyrate---2-oxoglutarate transaminase, which can supply the substrate for this enzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
110277-62-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC19606
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Manually annotated by BRENDA team
N-terminal amino acid sequence; strain ATCC23055
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain ATCC 8090
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Manually annotated by BRENDA team
strain NCTC 10006
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Manually annotated by BRENDA team
strain ATCC 13047
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Manually annotated by BRENDA team
strain ATCC 13182
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Manually annotated by BRENDA team
strain ATCC 13882
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Manually annotated by BRENDA team
strain ATCC 27155
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Manually annotated by BRENDA team
strain NCMB701
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Manually annotated by BRENDA team
strain NCMB701
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Manually annotated by BRENDA team
strain RM 2-Ia
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Manually annotated by BRENDA team
strain RM 2-Ia
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Manually annotated by BRENDA team
strain ATCC 13880
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Manually annotated by BRENDA team
ATCC17749
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Manually annotated by BRENDA team
strain NCMB6
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Manually annotated by BRENDA team
strain NCMB6
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Manually annotated by BRENDA team
Vibrio cholerae El Tor
El Tor strain
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Manually annotated by BRENDA team
Vibrio cholerae NCTC4716
strain NCTC4716, non-O1
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Manually annotated by BRENDA team
strain ATCC15338
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Manually annotated by BRENDA team
strain ATCC15338
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-aminobutanoate
propylamine + CO2
show the reaction diagram
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?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartic beta-semialdehyde + L-glutamic acid
show the reaction diagram
the enzyme is highly specific for 2-oxoglutarate
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r
L-2,4-diaminobutyrate
? + CO2
show the reaction diagram
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
L-ornithine
1,4-diaminobutane + 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-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
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activates 7fold at 20 mM
Mn2+
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activates 5fold at 20 mM
Zn2+
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activates 3fold at 20 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
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over 90% inhibition at 1 mM
Ca2+
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10% inhibition at 1 mM
carboxymethoxylamine
Cu2+
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highly inhibitory at 20 mM
Hg2+
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over 90% inhibition at 1 mM
Pb2+
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highly inhibitory at 20 mM
propane-1,3-diamine
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product inhibition, about 50% at 5 mM
Sn2+
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highly inhibitory at 20 mM
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DTT
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activates 8fold at 5-7 mM
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
DL-2,4-diaminobutanoate
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pH 8.3, 37C
0.081 - 1.51
L-2,4-diaminobutanoate
0.17
L-2,4-diaminobutyrate
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DABA AT/DC fusion protein
0.3
L-lysine
at pH 7.5 and 30C
11.1
L-ornithine
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DABA AT/DC fusion protein
0.3 - 1.2
Mg2+
0.0056
pyridoxal 5'-phosphate
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pH 8.3, 37C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.34
L-2,4-diaminobutanoate
Anabaena variabilis
Q3M985
at pH 7.5 and 30C
8.3
L-2,4-diaminobutyrate
Vibrio cholerae
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DABA AT//DC fusion protein
0.008
L-lysine
Anabaena variabilis
Q3M985
at pH 7.5 and 30C
0.54
L-ornithine
Vibrio cholerae
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DABA AT/DC fusion protein
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
630
L-2,4-diaminobutanoate
Anabaena variabilis
Q3M985
at pH 7.5 and 30C
2561
49
L-2,4-diaminobutyrate
Vibrio cholerae
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DABA AT/DC fusion protein
5984
26
L-lysine
Anabaena variabilis
Q3M985
at pH 7.5 and 30C
134
0.049
L-ornithine
Vibrio cholerae
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DABA AT/DC fusion protein
192
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00036
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cell extract
0.00071
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cell extract
0.0011
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cell extract
0.0014
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cell extract
0.0022
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enzyme in cell extract
0.0039
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enzyme in cell extract
0.00392
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enzyme in cell extract
0.0042
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enzyme in cell extract
0.005
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enzyme in cell extract
0.0051
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enzyme in cell extract
0.0052
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enzyme in cell extract
0.0071
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enzyme in cell extract
0.012
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recombinant enzyme in Escherichia coli
0.76
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partially purified enzyme
1.2
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partially purified enzyme
3.9
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purified enzyme
4.21
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purified enzyme
11.8
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purified enzyme
17.2
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purified enzyme
29.5
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partially purified enzyme
additional information
DABA AT activity compared to other Acinetobacter strains
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.8
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broad optimum
8 - 8.2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 10
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about half maximal activity at pH 6.5 and pH 9.3
6 - 9
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43% of maximal activity at pH 7.3, 60% at pH 9.0
7.2 - 8.2
7.8 - 9.3
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half maximal activity at pH 7.8 and pH 9.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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maximal growth temperature of the organism is 44C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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isoelectric focusing
5.2
amino acid sequence calculation
6.8
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
108000
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gel filtration
450000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 109000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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completely stable for up to 90 min
45
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loss of 18% and 55% after 30 min and 2 h, respectively
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes at below 0.1 mg/ml
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freezing and thawing of purified enzyme causes severe loss of activity
freezing and thawing of the purified enzyme causes almost complete loss of activity
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pyridoxal 5'-phosphate is required for stability during storage
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
1C, purified enzyme, 20 mM potassium phosphate, pH 7.5, 0.04 mM pyridoxal 5'-phosphate, and 0.02% NaN3, 2 weeks without loss of activity
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1C, purified enzyme, 20 mM potassium phosphate, pH 7.5, 0.04 mM pyridoxal 5'-phosphate, and 0.02% NaN3, loss of 65% activity within 1 week
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4C, purified enzyme, pH 7.5, in presence of pyridoxal 5'-phosphate and NaN3, 3 weeks, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3660fold to homogeneity by ammonium sulfate fractionation, gel filtration, and two steps of ion exchange chromatography
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DABA AT/DC affinity-purified
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HiTrap chelating column chromatography, and gel filtration
native enzyme 168fold by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
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native enzyme 1750fold to homogeneity by two steps of ion exchange chromatography, gel filtration, hydroxyapatite chromatography, and another two steps of ion exchange chromatography
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native enzyme 2150fold to homogeneity by ammonium sulfate fractionation, two steps of ion exchange chromatography, and two steps of gel filtration
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native enzyme 22.7fold by ammonium sulfate fractionation and anion exchange chromatography
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native enzyme 360fold
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native enzyme 886fold to homogeneity by two steps of ion exchange chromatography, gel filtration, hydroxyapatite chromatography, and another two steps of ion exchange chromatography
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recombinant enzyme from Escherichia coli strain HB101
recombinant enzyme from Escherichia coli strain HB101 to homogeneity by ammonium sulfate fractionation, ion exchange chromatography, gel filtration, and hydroxylapatite chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain HB101
DNA sequence determination and analysis, promoter determination, restriction mapping, functional expression in Escherichia coli strain XL1-Blue
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fusion protein DABA AT/DC cloned into pET28 vector, expressed in Escherichia coli BL21(DE3)
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gene dat, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain HB101
gene ddc, DNA and amino acid sequence determination and analysis, restriction mapping, expression in Escherichia coli strain HB101
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K198R
site-directed mutagenesis, mutant shows 96% of the wild-type activity
K307R
site-directed mutagenesis, mutant is catalytically inactive and shows slightly reduced molecular weight compared to the wild-type enzyme due to lacking pyridoxal 5'-phosphate
Show AA Sequence (471 entries)
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