Information on EC 4.1.1.86 - diaminobutyrate decarboxylase

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The expected taxonomic range for this enzyme is: Gammaproteobacteria

EC NUMBER
COMMENTARY
4.1.1.86
-
RECOMMENDED NAME
GeneOntology No.
diaminobutyrate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-2,4-diaminobutanoate = propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glycine, serine and threonine metabolism
-
Microbial metabolism in diverse environments
-
norspermidine biosynthesis
-
rhizobactin 1021 biosynthesis
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DABA aminotransferase/decarboxylase
-
-
DABA aminotransferase/decarboxylase
Vibrio cholerae El Tor
-
-
-
DABA AT
P56744
-
DABA AT/DC
-
-
DABA AT/DC
Vibrio cholerae El Tor
-
-
-
DABA DC
Q43908
-
DABA DC
Acinetobacter baumannii ATCC19606
-
;
-
DABA DC
Acinetobacter calcoaceticus ATCC23055
-
-
-
DABA DC
Q9S0P8
-
DABA DC
Serratia liquefaciens RM 2-Ia
-
-
-
DABA decarboxylase
-
-
DABA decarboxylase
Acinetobacter calcoaceticus ATCC23055
-
-
-
DABA decarboxylase
-
-
DABA decarboxylase
Listonella anguillarum NCMB6
-
-
-
DABA decarboxylase
-
-
DABA decarboxylase
Salinivibrio costicola NCMB701
-
-
-
DABA decarboxylase
-
-
DABA decarboxylase
Vibrio alginolyticus ATCC17749
-
-
-
DABA decarboxylase
-
-
DABA decarboxylase
Vibrio cholerae NCTC4716
-
-
-
DABA decarboxylase
-
-
DABA decarboxylase
Vibrio proteolyticus ATCC15338
-
-
-
DABA-DC
Enterobacter aerogenes NCTC 10006
-
-
-
L-2,4-diaminobutyrate aminotransferase/decarboxylase
-
-
L-2,4-diaminobutyrate aminotransferase/decarboxylase
Vibrio cholerae El Tor
-
-
-
L-2,4-diaminobutyrate decarboxylase
-
-
L-2,4-diaminobutyrate decarboxylase
Q43908
-
L-2,4-diaminobutyrate decarboxylase
Acinetobacter baumannii ATCC19606
-
;
-
L-2,4-diaminobutyrate decarboxylase
-
-
L-2,4-diaminobutyrate decarboxylase
Acinetobacter calcoaceticus ATCC23055
-
-
-
L-2,4-diaminobutyrate decarboxylase
-
-
L-2,4-diaminobutyrate decarboxylase
Q9S0P8
-
L-2,4-diaminobutyrate decarboxylase
Serratia liquefaciens RM 2-Ia
-
-
-
L-2,4-diaminobutyrate decarboxylase
-
-
L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase
P56744
-
L-2,4-diaminobutyric acid decarboxylase
-
-
L-2,4-diaminobutyric acid decarboxylase
Enterobacter aerogenes NCTC 10006
-
-
-
L-2,4-diaminobutyric acid decarboxylase
-
-
L-2,4-diaminobutyric acid decarboxylase
Listonella anguillarum NCMB6
-
-
-
L-2,4-diaminobutyric acid decarboxylase
-
-
L-2,4-diaminobutyric acid decarboxylase
Salinivibrio costicola NCMB701
-
-
-
L-2,4-diaminobutyric acid decarboxylase
-
-
L-2,4-diaminobutyric acid decarboxylase
Vibrio alginolyticus ATCC17749
-
-
-
L-2,4-diaminobutyric acid decarboxylase
-
-
L-2,4-diaminobutyric acid decarboxylase
Vibrio cholerae NCTC4716
-
-
-
L-2,4-diaminobutyric acid decarboxylase
-
-
L-2,4-diaminobutyric acid decarboxylase
Vibrio proteolyticus ATCC15338
-
-
-
additional information
P56744
the enzyme belongs to the subgroup II of the aminotransferases
CAS REGISTRY NUMBER
COMMENTARY
110277-62-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ATCC 19606, gene dat
SwissProt
Manually annotated by BRENDA team
strain ATCC19606
-
-
Manually annotated by BRENDA team
Acinetobacter baumannii ATCC19606
strain ATCC19606
-
-
Manually annotated by BRENDA team
N-terminal amino acid sequence; strain ATCC23055
-
-
Manually annotated by BRENDA team
strains ATCC23055 and IFO12552
-
-
Manually annotated by BRENDA team
Acinetobacter calcoaceticus ATCC23055
N-terminal amino acid sequence; strain ATCC23055
-
-
Manually annotated by BRENDA team
strain ATCC 8090
-
-
Manually annotated by BRENDA team
gene ddc
SwissProt
Manually annotated by BRENDA team
strain ATCC 13048
-
-
Manually annotated by BRENDA team
strain NCTC 10006
-
-
Manually annotated by BRENDA team
Enterobacter aerogenes NCTC 10006
strain NCTC 10006
-
-
Manually annotated by BRENDA team
strain ATCC 13047
-
-
Manually annotated by BRENDA team
strain ATCC 13182
-
-
Manually annotated by BRENDA team
strain ATCC 13882
-
-
Manually annotated by BRENDA team
strain NCMB6
-
-
Manually annotated by BRENDA team
Listonella anguillarum NCMB6
strain NCMB6
-
-
Manually annotated by BRENDA team
strain ATCC 27155
-
-
Manually annotated by BRENDA team
strain NCMB701
-
-
Manually annotated by BRENDA team
Salinivibrio costicola NCMB701
strain NCMB701
-
-
Manually annotated by BRENDA team
strain RM 2-Ia
-
-
Manually annotated by BRENDA team
Serratia liquefaciens RM 2-Ia
strain RM 2-Ia
-
-
Manually annotated by BRENDA team
strain ATCC 13880
-
-
Manually annotated by BRENDA team
Vibrio alginolyticus ATCC17749
ATCC17749
-
-
Manually annotated by BRENDA team
El Tor strain
-
-
Manually annotated by BRENDA team
strain NCTC4716, non-O1
-
-
Manually annotated by BRENDA team
Vibrio cholerae El Tor
El Tor strain
-
-
Manually annotated by BRENDA team
Vibrio cholerae NCTC4716
strain NCTC4716, non-O1
-
-
Manually annotated by BRENDA team
strain ATCC15338
-
-
Manually annotated by BRENDA team
Vibrio proteolyticus ATCC15338
strain ATCC15338
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
the DABA AT/DC fusion protein is responsible for diaminopropane production
physiological function
Vibrio cholerae El Tor
-
the DABA AT/DC fusion protein is responsible for diaminopropane production
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-aminobutanoate
propylamine + CO2
show the reaction diagram
-, P56744
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Q9S0P8
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-, P56744
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
GC-MS product identification
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
specific for
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
propane-1,3-diamine is a precursor for norspermidine, the enzyme is involved in biosynthesis of norspermidine
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
the enzyme is involved in polyamine biosynthesis
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
stereospecific reaction, no activity with the D-isomer
product identification
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Vibrio cholerae NCTC4716, Listonella anguillarum NCMB6
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Serratia liquefaciens RM 2-Ia
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Enterobacter aerogenes NCTC 10006
-
-, the enzyme is involved in polyamine biosynthesis
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Acinetobacter calcoaceticus ATCC23055
-
-, specific for
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Acinetobacter baumannii ATCC19606
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Salinivibrio costicola NCMB701, Vibrio alginolyticus ATCC17749
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Vibrio alginolyticus ATCC17749
-
stereospecific reaction, no activity with the D-isomer
product identification
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Vibrio proteolyticus ATCC15338
-
-
-
-
?
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartic beta-semialdehyde + L-glutamic acid
show the reaction diagram
-, P56744
the enzyme is highly specific for 2-oxoglutarate
-
-
r
L-2,4-diaminobutyrate
? + CO2
show the reaction diagram
Vibrio cholerae, Vibrio cholerae El Tor
-
DABA AT/DC fusion protein exhibits a preference for L-2,4-diaminobutyrate over L-ornithine by 1000fold
-
-
?
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
-, P56744
-
-
-
?
L-ornithine
1,4-diaminobutane + CO2
show the reaction diagram
-, P56744
low activity
-
-
?
L-ornithine
1,4-diaminobutane + CO2
show the reaction diagram
Vibrio cholerae, Vibrio cholerae El Tor
-
Kcat/Km is 1000fold lower than with L-2,4-diaminobutyrate
-
-
?
additional information
?
-
-
no activity with 2,3-diaminopropionate, ornithine, lysine, or arginine
-
-
-
additional information
?
-
-
no activity with 4-N-acetyl-L-2,4-diaminobutanoate, L-2,3-diaminopropionate, L-ornithine, and L-lysine
-
-
-
additional information
?
-
-, P56744
substrate specificity of the purified recombinant enzyme, L-2,3-diaminopropionic acid is a poor substrate
-
-
-
additional information
?
-
Acinetobacter calcoaceticus ATCC23055
-
no activity with 4-N-acetyl-L-2,4-diaminobutanoate, L-2,3-diaminopropionate, L-ornithine, and L-lysine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Q9S0P8
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-, P56744
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
propane-1,3-diamine is a precursor for norspermidine, the enzyme is involved in biosynthesis of norspermidine
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
-
the enzyme is involved in polyamine biosynthesis
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Vibrio cholerae NCTC4716, Listonella anguillarum NCMB6
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Serratia liquefaciens RM 2-Ia
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Enterobacter aerogenes NCTC 10006
-
the enzyme is involved in polyamine biosynthesis
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Acinetobacter calcoaceticus ATCC23055
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Acinetobacter baumannii ATCC19606
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
Salinivibrio costicola NCMB701, Vibrio alginolyticus ATCC17749, Vibrio proteolyticus ATCC15338
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q9S0P8
binds to Lys307
pyridoxal 5'-phosphate
-
maximal activity at 0.1 mM PLP
pyridoxal 5'-phosphate
-
absolutely required for activity, highly activating in pesence of 20 mM Mg2+
pyridoxal 5'-phosphate
-
required, depletion leads to over 25% irreversible loss of activity
pyridoxal 5'-phosphate
-
maximal activity at 0.1 mM PLP, depletion leads to irreversible loss of 70% activity
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
about 65% of the activity with Mg2+
Ca2+
-
activates 14fold at 20 mM
Ca2+
-
activates, preferred divalent cation
Cu2+
-
activates 7fold at 20 mM
Mg2+
-
required, activates 7fold at 10 mM
Mg2+
-
required, activates 17fold at 10 mM
Mg2+
-
30% activation at 20 mM
Mg2+
-
required, activates 20fold at 20 mM, enhances activation by PLP
Mg2+
-
stimulates 30% at 20 mM
Sr2+
-
about 65% of the activity with Mg2+
Zn2+
-
activates 3fold at 20 mM
Mn2+
-
activates 5fold at 20 mM
additional information
-
enzyme is not affected by Ca2+
additional information
-
no effect by Na+ and K+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ag+
-
over 90% inhibition at 1 mM
Ca2+
-
10% inhibition at 1 mM
carboxymethoxylamine
-
PLP-dependent inhibitor, 42% inibition at 0.5 mM, 78% inhibition at 1 mM
carboxymethoxylamine
-
PLP-dependent inhibitor, 42% inibition at 0.5 mM, 65% inhibition at 1 mM
Co2+
-
highly inhibitory at 20 mM
Cu2+
-
highly inhibitory at 20 mM
Fe2+
-
highly inhibitory at 20 mM
-
Fe2+
-
over 90% inhibition at 1 mM
-
Hg2+
-
over 90% inhibition at 1 mM
Mn2+
-
highly inhibitory at 20 mM
Pb2+
-
highly inhibitory at 20 mM
propane-1,3-diamine
-
product inhibition, about 50% at 5 mM
Sn2+
-
highly inhibitory at 20 mM
Zn2+
-
highly inhibitory at 20 mM
Zn2+
-
over 90% inhibition at 1 mM
additional information
-
no inhibition by N-ethylmaleimide at up to 20 mM
-
additional information
-
the enzyme is not affected by GTP, ATP, DTT, Na+ or K+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
DTT
-
activates 8fold at 5-7 mM
additional information
-
no activation by ATP or GTP
-
additional information
-
L-2,4-diaminobutanoate induces enzyme expression
-
additional information
-
L-2,4-diaminobutanoate induces enzyme expression
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.3
-
DL-2,4-diaminobutanoate
-
pH 8.3, 37C
0.081
-
L-2,4-diaminobutanoate
-
pH 8.3, 37C
0.13
-
L-2,4-diaminobutanoate
-
pH 8.3, 37C
0.32
-
L-2,4-diaminobutanoate
-
pH 8.0, 37C
0.32
-
L-2,4-diaminobutanoate
-
pH 8.3, 37C
0.91
-
L-2,4-diaminobutanoate
-
pH 8.5, 37C
1.07
-
L-2,4-diaminobutanoate
-
pH 8.0, 37C
1.51
-
L-2,4-diaminobutanoate
-
pH 8.5, 37C
0.17
-
L-2,4-diaminobutyrate
-
DABA AT/DC fusion protein
11.1
-
L-ornithine
-
DABA AT/DC fusion protein
0.3
-
Mg2+
-
pH 8.0, 37C
1.2
-
Mg2+
-
pH 8.0, 37C
0.0056
-
pyridoxal 5'-phosphate
-
pH 8.3, 37C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8.3
-
L-2,4-diaminobutyrate
-
DABA AT//DC fusion protein
0.54
-
L-ornithine
-
DABA AT/DC fusion protein
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
49
-
L-2,4-diaminobutyrate
-
DABA AT/DC fusion protein
11966
0.049
-
L-ornithine
-
DABA AT/DC fusion protein
12348
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00036
-
-
cell extract
0.00071
-
-
cell extract
0.0011
-
-
cell extract
0.0014
-
-
cell extract
0.0022
-
-
enzyme in cell extract
0.0039
-
-
enzyme in cell extract
0.00392
-
-
enzyme in cell extract
0.0042
-
-
enzyme in cell extract
0.005
-
-
enzyme in cell extract
0.0051
-
-
enzyme in cell extract
0.0052
-
-
enzyme in cell extract
0.0071
-
-
enzyme in cell extract
0.012
-
-
recombinant enzyme in Escherichia coli
0.76
-
-
partially purified enzyme
1.2
-
-
partially purified enzyme
3.9
-
-
purified enzyme
4.21
-
-
purified enzyme
11.8
-
-
purified enzyme
17.2
-
-
purified enzyme
29.5
-
-
partially purified enzyme
additional information
-
P56744
DABA AT activity compared to other Acinetobacter strains
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
10
-
about half maximal activity at pH 6.5 and pH 9.3
6
9
-
43% of maximal activity at pH 7.3, 60% at pH 9.0
7.2
8.2
-
narrow pH range, the enzyme is almost inactive at pH 7.0
7.8
9.3
-
half maximal activity at pH 7.8 and pH 9.3
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
P56744
assay at
37
-
-
assay at
additional information
-
-
maximal growth temperature of the organism is 44C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
isoelectric focusing
5.2
-
Q43908
amino acid sequence calculation
6.8
-
-
isoelectric focusing
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
108000
-
-
gel filtration
450000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
P56744
x * 47423, DNA sequence calculation
?
-
x * 53000, approximately, SDS-PAGE
?
Q9S0P8
x * 53659, DNA sequence calculation
?
-
x * 53000, recombinant enzyme, SDS-PAGE
?
Acinetobacter baumannii ATCC19606
-
x * 53000, approximately, SDS-PAGE; x * 53000, recombinant enzyme, SDS-PAGE
-
dimer
-
2 * 51000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
Acinetobacter calcoaceticus ATCC23055
-
2 * 53000, SDS-PAGE
-
tetramer
-
4 * 109000, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
stable for 12 h at 4C in 20 mM potassium phosphate
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
completely stable for up to 90 min
40
-
-
stable up to, purified enzyme
40
-
-
purified enzyme, stable for more than 15 min at pH 8.5
45
-
-
loss of 18% and 55% after 30 min and 2 h, respectively
50
-
-
above, rapid inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing and thawing of purified enzyme causes severe loss of activity
-
bovine serum albumin stabilizes at below 0.1 mg/ml
-
freezing and thawing of the purified enzyme causes almost complete loss of activity
-
pyridoxal 5'-phosphate is required for stability during storage
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
4C, purified enzyme, pH 7.5, in presence of pyridoxal 5'-phosphate and NaN3, 3 weeks, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme from Escherichia coli strain HB101
Q43908
recombinant enzyme from Escherichia coli strain HB101 to homogeneity by ammonium sulfate fractionation, ion exchange chromatography, gel filtration, and hydroxylapatite chromatography
P56744
native enzyme 168fold by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
-
native enzyme 2150fold to homogeneity by ammonium sulfate fractionation, two steps of ion exchange chromatography, and two steps of gel filtration
-
native enzyme 1750fold to homogeneity by two steps of ion exchange chromatography, gel filtration, hydroxyapatite chromatography, and another two steps of ion exchange chromatography
-
native enzyme 360fold
-
native enzyme 886fold to homogeneity by two steps of ion exchange chromatography, gel filtration, hydroxyapatite chromatography, and another two steps of ion exchange chromatography
-
3660fold to homogeneity by ammonium sulfate fractionation, gel filtration, and two steps of ion exchange chromatography
-
native enzyme 22.7fold by ammonium sulfate fractionation and anion exchange chromatography
-
DABA AT/DC affinity-purified
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain HB101
Q43908
DNA sequence determination and analysis, promoter determination, restriction mapping, functional expression in Escherichia coli strain XL1-Blue
-
gene dat, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain HB101
P56744
gene ddc, DNA and amino acid sequence determination and analysis, restriction mapping, expression in Escherichia coli strain HB101
Q9S0P8
fusion protein DABA AT/DC cloned into pET28 vector, expressed in Escherichia coli BL21(DE3)
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K198R
Q9S0P8
site-directed mutagenesis, mutant shows 96% of the wild-type activity
K307R
Q9S0P8
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