Information on EC 2.6.1.48 - 5-aminovalerate transaminase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.6.1.48
-
RECOMMENDED NAME
GeneOntology No.
5-aminovalerate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-aminopentanoate + 2-oxoglutarate = 5-oxopentanoate + L-glutamate
show the reaction diagram
A pyridoxal-phosphate protein
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine degradation III
-
-
L-lysine degradation IV
-
-
L-lysine degradation X
-
-
Lysine degradation
-
-
lysine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
5-aminopentanoate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
37277-97-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CBS 8109
-
-
Manually annotated by BRENDA team
Candida famata CBS 8109
CBS 8109
-
-
Manually annotated by BRENDA team
ATCC 20366
-
-
Manually annotated by BRENDA team
CBS 621
-
-
Manually annotated by BRENDA team
var.membranaefaciens
-
-
Manually annotated by BRENDA team
no activity in Candida boidinii
CBS 5777
-
-
Manually annotated by BRENDA team
no activity in Candida boidinii CBS 5777
CBS 5777
-
-
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
NCYC 61
-
-
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
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
show the reaction diagram
5-aminopentanoate + 2-oxoglutarate
5-oxovalerate + L-glutamate
show the reaction diagram
6-aminohexanoate + 2-oxoglutarate
adipic semialdehyde + L-glutamate
show the reaction diagram
glycine + 2-oxoglutarate
glyoxalate + L-glutamate
show the reaction diagram
-
relative activity 1%
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
relative activity 10%
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
show the reaction diagram
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
5-aminopentanoate + 2-oxoglutarate
5-oxovalerate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Diaminopropionate
-
noncompetitive inhibition with respect to delta-aminovalerate, competitive inhibition to 2-oxoglutarate
2,4-diaminobutyrate
-
noncompetitive inhibition with respect to delta-aminovalerate, competitive inhibition to 2-oxoglutarate
alanine
-
noncompetitive inhibition with respect to delta-aminovalerate, competitive inhibition to 2-oxoglutarate
beta-Alanine
-
noncompetitive inhibition with respect to delta-aminovalerate, competitive inhibition to 2-oxoglutarate
glycine
-
noncompetitive inhibition with respect to delta-aminovalerate, competitive inhibition to 2-oxoglutarate
hydroxylamine
-
-
L-lysine
-
noncompetitive inhibition with respect to delta-aminovalerate, competitive inhibition to 2-oxoglutarate
L-ornithine
-
mixed inhibition with respect to delta-aminovalerate, competitive inhibition to 2-oxoglutarate
p-chloromercuribenzoate
-
-
Semicarbazide
-
-
additional information
-
alpha-aminobutyrate, 4-aminobutyrate, alpha-aminovalerate and epsilon-aminocaproate does not cause any inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.6 - 8
2-oxoglutarate
4 - 10
delta-aminovaleric acid
4.1
glutamic acid
-
pH 8.0, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7 - 50
2,3-Diaminopropionate
11.5 - 190
2,4-diaminobutyrate
15 - 120
alanine
5 - 16
beta-Alanine
10 - 90
glycine
12.5
L-lysine
-
pH 7.8, 35C, competitive inhibition with respect to 2-oxoglutarate
5.6
L-ornithine
-
pH 7.8, 35C, competitive inhibition with respect to 2-oxoglutarate
120
lysine
-
pH 7.8, 35C, noncompetitive inhibition with respect to delta-aminovalerate
9.5
ornithine
-
pH 7.8, 35C, mixed inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
-
half-maximal rates at pH 6.5 and 9.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 55
-
maximal activity at 55, 45 and 40C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
SDS-PAGE; x * 46000, SDS-PAGE
46290
calculated from amino acid sequence
60000
-
2 * 60000, SDS-PAGE
118000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 46000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
preserves 50% of its activity after being heated for 7 min, in presence of 2-oxoglutarate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate and protects against thermal denaturation
-
2-oxoglutarate and pyridoxal 5'-phosphate protects against thermal denaturation
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-Bind column chromatography; recombinant
partially
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned by PCR and expressed in Escherichia coli as a C-terminal histidine-tagged fusion protein; expressed in Escherichia coli BL21(DE3) cells
gene davT identified using a transposon to generate transcriptional fusions by insertional mutagenesis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
production of 5-aminovalerate and glutarate in Escherichia coli. Endogenous over-production of the precursor, lysine, is first achieved through metabolic deregulation of its biosynthesis pathway by introducing feedback resistant mutants of aspartate kinase III and dihydrodipicolinate synthase. Further disruption of native lysine decarboxylase activity limits cadaverine by-product formation. Co-expression of lysine monooxygenase and 5-aminovaleramide amidohydrolase then results in the production of 0.86 g/l 5-aminovalerate in 48 h. The additional co-expression of glutaric semialdehyde dehydrogenase and 5-aminovalerate aminotransferase leads to the production of 0.82 g/l glutarate under the same conditions. Yields on glucose are 71 and 68 mmol/mol for 5-aminovalerate and glutarate, respectively
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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