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Information on EC 2.6.1.76 - diaminobutyrate-2-oxoglutarate transaminase
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EC Tree
2.6.1.76 diaminobutyrate-2-oxoglutarate transaminaseIUBMB Comments
A pyridoxal-phosphate protein that requires potassium for activity . 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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Word Map
- 2.6.1.76
- medicine
- 1,3-diaminopropane
- ectoine
-
halophilic
-
methanotrophs
-
halotolerant
- methanol
- acinetobacter
-
osmoadaptation
-
alcaliphilum
- baumannii
- aminotransferases
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
daba at, daba aminotransferase, l-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase, diaminobutyrate transaminase, 2,4-diaminobutyrate aminotransferase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(Pl)EctB
2,4-diaminobutyrate 4-aminotransferase
-
-
-
-
DABA aminotransferase
DABA AT
-
-
-
-
DABA-AT
-
-
-
-
DABA:2-KG 4 aminotransferase
-
-
-
-
Diaminobutyrate transaminase
-
-
-
-
EctB
L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase
-
-
-
-
L-diaminobutyric acid transaminase
-
-
-
-
additional information
DABA aminotransferase
-
-
-
-
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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
-
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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PATHWAY SOURCE
PATHWAYS
BRENDA
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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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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
-
-
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
-
-
-
r
L-aspartate 4-semialdehyde + L-homoserine
L-2,4-diaminobutanoate + 4-hydroxy-2-oxobutanoic acid
about 5% of the activity with L-glutamate
-
-
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
-
-
r
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
-
-
-
?
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-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
-
-
-
?
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
preferred enzyme
-
-
?
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
Paenibacillus lautus Y412MC10
-
-
-
?
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
Paenibacillus lautus Y412MC10
preferred enzyme
-
-
?
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
-
-
-
-
?
additional information
?
-
no substrates: L-alanine, L-aspartate, L-lysine
-
-
?
additional information
?
-
(Pl)EctB also catalyzes a GABA-TA-type reaction, EC 2.6.1.19, but with less activity
-
-
-
additional information
?
-
Paenibacillus lautus Y412MC10
(Pl)EctB also catalyzes a GABA-TA-type reaction, EC 2.6.1.19, but with less activity
-
-
-
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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 + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
-
-
-
?
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
Paenibacillus lautus Y412MC10
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
PLP, residue Lys274 attaches the PLP cofactor to enzyme (Pl)EctB. The architecture of the PLP-binding site, formed by two monomeric subunits, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
activates slightly at up to 350 mM, inhibits by 50% at 1.25 M
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
activates slightly at up to 350 mM, inhibits by 50% at 1.25 M
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
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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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from the effluent of a hot spring in the Yellowstone National Park (United States)
UniProt
brenda
Paenibacillus lautus Y412MC10
isolated from the effluent of a hot spring in the Yellowstone National Park (United States)
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
MH020163
phylogenetic analysis of nucleotides and amino acids reveals that the ectA, B and C sequences of Bacillus clausii NIOT-DSB04 were conserved in many eubacteria
evolution
Alkalihalobacillus clausii NIOT-DSB04
-
phylogenetic analysis of nucleotides and amino acids reveals that the ectA, B and C sequences of Bacillus clausii NIOT-DSB04 were conserved in many eubacteria
-
metabolism
MH020163
the enzyme is involved in ectoine biosynthesis. Ectoine is a compatible solute, serves as a protective compound in many halophilic eubacterial cells under stress
metabolism
Alkalihalobacillus clausii NIOT-DSB04
-
the enzyme is involved in ectoine biosynthesis. Ectoine is a compatible solute, serves as a protective compound in many halophilic eubacterial cells under stress
-
additional information
structural homology modeling of (Pl)EctB using the crystal structure of the GABA transaminase from Arthrobacter aurescens (PDB ID 4ATP, EC 2.6.1.19) as template
additional information
Paenibacillus lautus Y412MC10
-
structural homology modeling of (Pl)EctB using the crystal structure of the GABA transaminase from Arthrobacter aurescens (PDB ID 4ATP, EC 2.6.1.19) as template
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
homotetramer
4 * 49100, recombinant Strep II-tagged enzyme, SDS-PAGE
homotetramer
Paenibacillus lautus Y412MC10
-
4 * 49100, recombinant Strep II-tagged enzyme, SDS-PAGE
-
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PROTEIN VARIANTS
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
-
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
-
K274A
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive
K274H
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive. This amino acid substitution does not affect the quaternary assembly of the mutant protein
K274R
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive
K274A
Paenibacillus lautus Y412MC10
-
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive
-
K274H
Paenibacillus lautus Y412MC10
-
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive. This amino acid substitution does not affect the quaternary assembly of the mutant protein
-
K274R
Paenibacillus lautus Y412MC10
-
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant Strep II-tagged enzyme from Escherichia coli by streptavidin-affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the expression vector pQE30 with a 6His-tag and expressed in Escherichia coli JM109 M15 cells
MH020163
gene ectB, genetic structure, recombinant overexpression of codon-optimized version of (Pl)ectB as N-terminally Strep II-tagged protein from modified plasmid pLC52 in Escherichia coli strain BL21 and TOP 10 cells
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
medicine
-
responsible for many human infections including otitis media, meningitis, epiglottis and pneumonia
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
-
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
-
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
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ikai, H.; Yamamoto, S.
Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii
J. Bacteriol.
179
5118-5125
1997
Acinetobacter baumannii, Acinetobacter calcoaceticus, Acinetobacter genospecies, Acinetobacter haemolyticus, Acinetobacter johnsonii, Acinetobacter junii, Acinetobacter lwoffii, Acinetobacter radioresistens, Acinetobacter radioresistens IAM13186
brenda
Ikai, H.; Yamamoto, S.
Two genes involved in the 1,3-diaminopropane production pathway in Haemophilus influenzae
Biol. Pharm. Bull.
21
170-173
1998
Acinetobacter baumannii, Haemophilus influenzae
brenda
Ono, H.; Sawada, K.; Khunajakr, N.; Tao, T.; Yamamoto, M.; Hiramoto, M.; Shinmyo, A.; Takano, M.; Murooka, Y.
Characterization of biosynthetic enzymes for ectoine as a compatible solute in a moderately halophilic eubacterium, Halomonas elongata
J. Bacteriol.
181
91-99
1999
Halomonas elongata (O52250)
brenda
Chen, W.; Zhang, S.; Jiang, P.; Yao, J.; He, Y.; Chen, L.; Gui, X.; Dong, Z.; Tang, S.Y.
Design of an ectoine-responsive AraC mutant and its application in metabolic engineering of ectoine biosynthesis
Metab. Eng.
30
149-155
2015
Halomonas elongata (O52250), Halomonas elongata DSM 2581 (O52250)
brenda
Anburajan, L.; Meena, B.; Vinithkumar, N.; Kirubagaran, R.; Dharani, G.
Functional characterization of a major compatible solute in Deep Sea halophilic eubacteria of active volcanic Barren Island, Andaman and Nicobar Islands, India
Infect. Genet. Evol.
73
261-265
2019
Alkalihalobacillus clausii (MH020163), Alkalihalobacillus clausii NIOT-DSB04 (MH020163)
brenda
Richter, A.A.; Mais, C.N.; Czech, L.; Geyer, K.; Hoeppner, A.; Smits, S.H.J.; Erb, T.J.; Bange, G.; Bremer, E.
Biosynthesis of the stress-protectant and chemical chaperon ectoine biochemistry of the transaminase EctB
Front. Microbiol.
10
2811
2019
Paenibacillus lautus (D3EKC0), Paenibacillus lautus Y412MC10 (D3EKC0)
brenda
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Release 2023.1 (January 2023)
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