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Enzyme Nomenclature
Information on EC 2.6.1.76 - diaminobutyrate-2-oxoglutarate transaminase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
2.6.1.76
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RECOMMENDED NAME
GeneOntology No.
diaminobutyrate-2-oxoglutarate transaminase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate
Involved in the formation of 1,3-diaminopropane in Haemophilus influenzae and Acinetobacter baumannii. A product of the ddc gene that also encodes L-2,4-diaminobutyrate decarboxylase in Acinetobacter baumannii. Differs from EC 2.6.1.46 diaminobutyrate-pyruvate transaminase, which has pyruvate as the amino-group acceptor
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L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-2,4-diaminobutanoate:2-oxoglutarate 4-aminotransferase
A pyridoxal-phosphate protein that requires potassium for activity [4]. In the proteobacterium Acinetobacter baumannii, this enzyme is cotranscribed with the neighbouring ddc gene that also encodes EC 4.1.1.86, diaminobutyrate decarboxylase. Differs from EC 2.6.1.46, diaminobutyrate---pyruvate transaminase, which has pyruvate as the amino-group acceptor. This is the first enzyme in the ectoine-biosynthesis pathway, the other enzymes involved being EC 2.3.1.178, diaminobutyrate acetyltransferase and EC 4.2.1.108, ectoine synthase [3,4].
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CAS REGISTRY NUMBER
COMMENTARY
196622-96-5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
4-aminobutanoate + 2-oxoglutarate
? + L-glutamate
about 60% of the activity with L-2,4-diaminobutanoate
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-
r
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
L-aspartate 4-semialdehyde + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
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-
-
r
L-aspartate 4-semialdehyde + L-homoserine
L-2,4-diaminobutanoate + 4-hydroxy-2-oxobutanoic acid
about 5% of the activity with L-glutamate
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-
r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-ornithine + 2-oxoglutarate
? + L-glutamate
about 6% of the activity with L-2,4-diaminobutanoate
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r
additional information
?
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no substrates: L-alanine, L-aspartate, L-lysine
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L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
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-
-
?
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
-
-
-
r
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
-
-
-
?
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
-
-
-
-
r
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
-
-
-
-
r
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
-
-
-
-
r
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
-
-
-
-
r
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
-
-
-
-
r
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
-
-
-
-
r
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
-
-
-
-
r
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
-
-
-
-
r
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
-
-
-
-
r
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
-
-
-
-
?
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
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-
-
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r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
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-
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r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
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-
-
-
r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
-
-
-
-
r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
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-
-
-
r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
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-
-
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r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
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-
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r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
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r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
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-
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r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
L-2,4-diaminobutanoate
mutant D180V/F320Y/Q325R , pH 8.5, 37°C
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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
5535
L-2,4-diaminobutanoate
mutant D180V/F320Y/Q325R , pH 8.5, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homologs of dat detected by PCR amplification
identification and analysis of the dat gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase with Escherichia coli transformants
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D180V
about 2fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
D180V/F320Y/Q325R
about 2.1-3.3fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
E36V
about 1.5fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
D180V
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about 2fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
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D180V/F320Y/Q325R
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about 2.1-3.3fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
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E36V
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about 1.5fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
medicine
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drug development, Acinetobacter sp. can be part of the normal flora of human skin but also of opportunistic infections like septicemia, pneumonia, endocarditis, meningitis, skin and wound sepsis or urinary tract infections, clinically important isolates show widespread and increasing resistance to many commonly used antibiotics
medicine
-
drug development, Acinetobacter sp. can be part of the normal flora of human skin but also of opportunistic infections like septicemia, pneumonia, endocarditis, meningitis, skin and wound sepsis or urinary tract infections, clinically important isolates show widespread and increasing resistance to many commonly used antibiotics
medicine
-
drug development, Acinetobacter sp. can be part of the normal flora of human skin but also of opportunistic infections like septicemia, pneumonia, endocarditis, meningitis, skin and wound sepsis or urinary tract infections, clinically important isolates show widespread and increasing resistance to many commonly used antibiotics
medicine
-
drug development, Acinetobacter sp. can be part of the normal flora of human skin but also of opportunistic infections like septicemia, pneumonia, endocarditis, meningitis, skin and wound sepsis or urinary tract infections, clinically important isolates show widespread and increasing resistance to many commonly used antibiotics
medicine
-
drug development, Acinetobacter sp. can be part of the normal flora of human skin but also of opportunistic infections like septicemia, pneumonia, endocarditis, meningitis, skin and wound sepsis or urinary tract infections, clinically important isolates show widespread and increasing resistance to many commonly used antibiotics
medicine
-
drug development, Acinetobacter sp. can be part of the normal flora of human skin but also of opportunistic infections like septicemia, pneumonia, endocarditis, meningitis, skin and wound sepsis or urinary tract infections, clinically important isolates show widespread and increasing resistance to many commonly used antibiotics
medicine
-
drug development, Acinetobacter sp. can be part of the normal flora of human skin but also of opportunistic infections like septicemia, pneumonia, endocarditis, meningitis, skin and wound sepsis or urinary tract infections, clinically important isolates show widespread and increasing resistance to many commonly used antibiotics
medicine
-
drug development, Acinetobacter sp. can be part of the normal flora of human skin but also of opportunistic infections like septicemia, pneumonia, endocarditis, meningitis, skin and wound sepsis or urinary tract infections, clinically important isolates show widespread and increasing resistance to many commonly used antibiotics
medicine
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responsible for many human infections including otitis media, meningitis, epiglottis and pneumonia
medicine
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drug development, Acinetobacter sp. can be part of the normal flora of human skin but also of opportunistic infections like septicemia, pneumonia, endocarditis, meningitis, skin and wound sepsis or urinary tract infections, clinically important isolates show widespread and increasing resistance to many commonly used antibiotics
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synthesis
production of ectoine in Escherichia coli. The Escherichia coli regulatory protein AraC is engineered to recognize ectoine as it snon-natural effector and to activate transcription upon ectoine binding. The ectoine biosynthetic cluster from Halomonas elongata is cloned into Escherichia coli. By engineering the rate-limiting enzyme L-2,4-diaminobutyric acid aminotransferase EctB, ectoine production and the specific activityof the EctB mutant are increased
synthesis
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production of ectoine in Escherichia coli. The Escherichia coli regulatory protein AraC is engineered to recognize ectoine as it snon-natural effector and to activate transcription upon ectoine binding. The ectoine biosynthetic cluster from Halomonas elongata is cloned into Escherichia coli. By engineering the rate-limiting enzyme L-2,4-diaminobutyric acid aminotransferase EctB, ectoine production and the specific activityof the EctB mutant are increased
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LINKS TO OTHER DATABASES (specific for EC-Number 2.6.1.76)
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