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Information on EC 4.1.1.86 - diaminobutyrate decarboxylase
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4.1.1.86 diaminobutyrate decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein that requires a divalent cation for activity . 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.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
daba dc, l-2,4-diaminobutyrate decarboxylase, daba decarboxylase, daba-dc, l-2,4-diaminobutyric acid decarboxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DABA aminotransferase/decarboxylase
DABA AT/DC
DABA DC
DABA decarboxylase
DABA-DC
L-2,4-diaminobutyrate aminotransferase/decarboxylase
L-2,4-diaminobutyrate decarboxylase
L-2,4-diaminobutyric acid decarboxylase
additional information
the enzyme belongs to the subgroup II of the aminotransferases
DABA aminotransferase/decarboxylase
Vibrio cholerae serotype O1 El Tor
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-
-
DABA AT/DC
Vibrio cholerae serotype O1 El Tor
-
-
-
DABA decarboxylase
Vibrio cholerae serotype O1 NCTC4716
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-
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L-2,4-diaminobutyrate aminotransferase/decarboxylase
Vibrio cholerae serotype O1 El Tor
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-
-
L-2,4-diaminobutyric acid decarboxylase
Vibrio cholerae serotype O1 NCTC4716
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-2,4-diaminobutanoate = propane-1,3-diamine + CO2
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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CAS REGISTRY NUMBER
COMMENTARY
110277-62-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartic beta-semialdehyde + L-glutamic acid
the enzyme is highly specific for 2-oxoglutarate
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-
r
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
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-
GC-MS product identification
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?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
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specific for
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-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
Acinetobacter calcoaceticus ATCC 23055
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specific for
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-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
-
the enzyme is involved in polyamine biosynthesis
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-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
Klebsiella aerogenes NCTC 10006
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the enzyme is involved in polyamine biosynthesis
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-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
-
propane-1,3-diamine is a precursor for norspermidine, the enzyme is involved in biosynthesis of norspermidine
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-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
-
stereospecific reaction, no activity with the D-isomer
product identification
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
-
stereospecific reaction, no activity with the D-isomer
product identification
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
Vibrio cholerae serotype O1 NCTC4716
-
-
-
-
?
L-2,4-diaminobutyrate
? + CO2
Vibrio cholerae serotype O1
-
DABA AT/DC fusion protein exhibits a preference for L-2,4-diaminobutyrate over L-ornithine by 1000fold
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-
?
L-2,4-diaminobutyrate
? + CO2
Vibrio cholerae serotype O1 El Tor
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DABA AT/DC fusion protein exhibits a preference for L-2,4-diaminobutyrate over L-ornithine by 1000fold
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-
?
L-lysine
1,5-diaminopentane + CO2
the catalytic efficiency of the enzyme is 24fold higher with L-2,4-diaminobutanoate than with L-lysine
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-
?
L-ornithine
1,4-diaminobutane + CO2
Vibrio cholerae serotype O1
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Kcat/Km is 1000fold lower than with L-2,4-diaminobutyrate
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-
?
L-ornithine
1,4-diaminobutane + CO2
Vibrio cholerae serotype O1 El Tor
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Kcat/Km is 1000fold lower than with L-2,4-diaminobutyrate
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?
additional information
?
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substrate specificity of the purified recombinant enzyme, L-2,3-diaminopropionic acid is a poor substrate
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?
additional information
?
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substrate specificity of the purified recombinant enzyme, L-2,3-diaminopropionic acid is a poor substrate
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?
additional information
?
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no activity with 4-N-acetyl-L-2,4-diaminobutanoate, L-2,3-diaminopropionate, L-ornithine, and L-lysine
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-
?
additional information
?
-
Acinetobacter calcoaceticus ATCC 23055
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no activity with 4-N-acetyl-L-2,4-diaminobutanoate, L-2,3-diaminopropionate, L-ornithine, and L-lysine
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?
additional information
?
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no activity with 2,3-diaminopropionate, ornithine, lysine, or arginine
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
-
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
-
the enzyme is involved in polyamine biosynthesis
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
Klebsiella aerogenes NCTC 10006
-
the enzyme is involved in polyamine biosynthesis
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
-
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
Vibrio cholerae serotype O1 NCTC4716
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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absolutely required for activity, highly activating in pesence of 20 mM Mg2+
pyridoxal 5'-phosphate
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maximal activity at 0.1 mM PLP, depletion leads to irreversible loss of 70% activity
pyridoxal 5'-phosphate
-
required, depletion leads to over 25% irreversible loss of activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Sr2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
carboxymethoxylamine
-
PLP-dependent inhibitor, 42% inhibition at 0.5 mM, 78% inhibition at 1 mM
carboxymethoxylamine
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PLP-dependent inhibitor, 42% inhibition at 0.5 mM, 65% inhibition at 1 mM
additional information
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no inhibition by N-ethylmaleimide at up to 20 mM
-
additional information
-
the enzyme is not affected by GTP, ATP, DTT, Na+ or K+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
L-2,4-diaminobutanoate induces enzyme expression
-
additional information
-
L-2,4-diaminobutanoate induces enzyme expression
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE