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 hide
2.6.1.46
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RECOMMENDED NAME
GeneOntology No.
diaminobutyrate-pyruvate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-2,4-diaminobutanoate + pyruvate = L-aspartate 4-semialdehyde + L-alanine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
L-2,4-diaminobutanoate:pyruvate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
37277-95-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain OUT300318
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Manually annotated by BRENDA team
strain DSM 1059
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Manually annotated by BRENDA team
strain 20Z
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Manually annotated by BRENDA team
gene pvdH
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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 + pyruvate
L-2-amino-4-oxobutanoate + L-alanine
show the reaction diagram
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-
-
r
L-2,4-diaminobutanoate + pyruvate
L-aspartate 4-semialdehyde + L-alanine
show the reaction diagram
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specificty for pyruvate is 41fold lower compared to 2-oxoglutarate
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r
L-2-amino-4-oxobutanoate + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
-
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r
L-2-amino-4-oxobutanoate + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
additional information
?
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enzyme is involved in biosynthesis of the pyoverdine siderophore
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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required for activity and stability
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydroxylamine
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3.3 mM: 87% inhibition, 0.33 mM: 58.3% inhibition, 0.033 mM: 16.6% inhibition
Semicarbazide hydrochloride
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20 mM: 83% inhibition, 10 mM: 63% inhibition
Sodium borohydride
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5 mM: complete inhibition
additional information
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EDTA has no effect
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
2-oxoglutarate
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pH 7.5, 25C, recombinant enzyme
0.26 - 0.29
L-2,4-diaminobutanoate
4.5
L-2-amino-4-oxobutanoate
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pH 8.5, 25C
1.2 - 9.1
L-glutamate
6.2
pyruvate
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pH 7.5, 25C, recombinant enzyme
additional information
additional information
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steady-state kinetic analysis, enzyme shows a ping-pong kinetic mechanism
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.39
2-oxoglutarate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00092
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2.21
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purified recombinant enzyme, coupled assay with homoserine dehydrogenase from Saccharomyces cerevisiae
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.6 - 8.7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
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gel filtration
183000
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recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 50000, recombinant enzyme, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, 100 mM 2,4-diaminobutyric acid
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
221fold, recombinantly overexpressed enzyme from Pseudomonas aeruginosa strain PAO1 by anion exchange chromatography and gel filtration to 90% purity
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ammonium sulfate fractionation
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ammonium sulfate precipitation, Sepharose CL-6B
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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gene pvdH, DNA sequence determination and analysis, subcloning and expression in Escherichia coli, overexpression in enzyme-knockout Pseudomonas aeruginosa strain PAO1
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