Information on EC 2.6.1.46 - diaminobutyrate-pyruvate transaminase

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The expected taxonomic range for this enzyme is: Gammaproteobacteria

EC NUMBER
COMMENTARY
2.6.1.46
-
RECOMMENDED NAME
GeneOntology No.
diaminobutyrate-pyruvate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-2,4-diaminobutanoate + pyruvate = L-aspartate 4-semialdehyde + L-alanine
show the reaction diagram
-
-
-
-
L-2,4-diaminobutanoate + pyruvate = L-aspartate 4-semialdehyde + L-alanine
show the reaction diagram
ping-pong kinetic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-2,4-diaminobutanoate:pyruvate aminotransferase
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aminotransferase, diaminobutyrate-pyruvate
-
-
-
-
DAB transaminase
-
-
DAB transaminase
-
-
-
diaminobutyrate-pyruvate aminotransferase
-
-
-
-
diaminobutyric acid transaminase
-
-
diaminobutyric acid transaminase
-
-
-
L-2,4-diaminobutyric acid aminotransferase
-
-
L-2,4-diaminobutyric acid aminotransferase
-
-
-
L-diaminobutyric acid transaminase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37277-95-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain DSM 2581
-
-
Manually annotated by BRENDA team
strain OUT300318
-
-
Manually annotated by BRENDA team
Halomonas elongata OUT300318
strain OUT300318
-
-
Manually annotated by BRENDA team
strain DSM 1059
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
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 + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
show the reaction diagram
-
2-oxoglutarate is the best amino donor substrate
-
-
r
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate + pyruvate
L-2-amino-4-oxobutanoate + L-alanine
show the reaction diagram
-
-
-
r
L-2,4-diaminobutanoate + pyruvate
L-aspartate 4-semialdehyde + L-alanine
show the reaction diagram
-
specificty for pyruvate is 41fold lower compared to 2-oxoglutarate
-
-
r
L-2-amino-4-oxobutanoate + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
-
-
-
?
L-2-amino-4-oxobutanoate + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
-
-
-
r
L-2-amino-4-oxobutanoate + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
-
involved in the biosynthesis of the osmolyte ectoine in halophilic eubacteria
-
?
L-2-amino-4-oxobutanoate + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
Halomonas elongata OUT300318, Halomonas elongata OUT30018
-
-
-
r
additional information
?
-
-
enzyme is involved in biosynthesis of the pyoverdine siderophore, no activity with 2-oxobutyrate as amino acceptor
-
-
-
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 + pyruvate
L-2-amino-4-oxobutanoate + L-alanine
show the reaction diagram
-
-
-
r
L-2-amino-4-oxobutanoate + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
-
-
-
r
L-2-amino-4-oxobutanoate + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
-
involved in the biosynthesis of the osmolyte ectoine in halophilic eubacteria
-
?
L-2-amino-4-oxobutanoate + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
Halomonas elongata OUT300318, Halomonas elongata OUT30018
-
-
-
r
additional information
?
-
-
enzyme is involved in biosynthesis of the pyoverdine siderophore
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
required for activity and stability
additional information
-
probably no need for heavy-metal ions
additional information
-
iron-limiting conditions induce pyoverdine siderophore biosynthesis including enzyme activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Semicarbazide hydrochloride
-
20 mM: 83% inhibition, 10 mM: 63% inhibition
Sodium borohydride
-
5 mM: complete inhibition
hydroxylamine
-
3.3 mM: 87% inhibition, 0.33 mM: 58.3% inhibition, 0.033 mM: 16.6% inhibition
additional information
-
EDTA has no effect
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.18
-
2-oxoglutarate
-
pH 7.5, 25C, recombinant enzyme
0.26
-
L-2,4-diaminobutanoate
-
pH 7.5, 25C, with 2-oxoglutarate, recombinant enzyme
0.29
-
L-2,4-diaminobutanoate
-
pH 7.5, 25C, with pyruvate, recombinant enzyme
4.5
-
L-2-amino-4-oxobutanoate
-
pH 8.5, 25C
1.2
-
L-glutamate
-
pH 9.1, 37C
1.85
-
L-glutamate
-
-
1.85
-
L-glutamate
-
pH 9.1, 37C
6.2
-
pyruvate
-
pH 7.5, 25C, recombinant enzyme
9.1
-
L-glutamate
-
pH 8.5, 25C
additional information
-
additional information
-
steady-state kinetic analysis, enzyme shows a ping-pong kinetic mechanism
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.39
-
2-oxoglutarate
-
pH 7.5, 25C, recombinant enzyme
1.39
-
pyruvate
-
pH 7.5, 25C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00092
-
-
-
2.21
-
-
purified recombinant enzyme, coupled assay with homoserine dehydrogenase from Saccharomyces cerevisiae
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
in presence of 0.4 M NaCl
25
-
-
assay at
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
44000
-
-
gel filtration
183000
-
-
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
tetramer
-
4 * 50000, recombinant enzyme, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, 100 mM 2,4-diaminobutyric acid
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, Sepharose CL-6B
-
221fold, recombinantly overexpressed enzyme from Pseudomonas aeruginosa strain PAO1 by anion exchange chromatography and gel filtration to 90% purity
-
ammonium sulfate fractionation
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
gene pvdH, DNA sequence determination and analysis, subcloning and expression in Escherichia coli, overexpression in enzyme-knockout Pseudomonas aeruginosa strain PAO1
-