Information on EC 2.6.1.17 - succinyldiaminopimelate transaminase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
2.6.1.17
-
RECOMMENDED NAME
GeneOntology No.
succinyldiaminopimelate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-L-2-amino-6-oxoheptanedioate + L-glutamate
show the reaction diagram
A pyridoxal-phosphate protein
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Lysine biosynthesis
-
lysine biosynthesis I
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
N-succinyl-L-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aminotransferase, succinyldiaminopimelate
-
-
-
-
DAP-AT
-
-
-
-
N-succinyl-L-diaminopimelic-glutamic transaminase
-
-
-
-
succinyldiaminopimelate aminotransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9030-46-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
no activity in Brewer's yeast
-
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus casei
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus sp.
-
-
-
Manually annotated by BRENDA team
no activity in Sus scrofa
-
-
-
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
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
O53870
-
-
-
?
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
Q9ZEX3
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
i.e. N-succinyl-alpha-amino-epsilon-ketopimelic acid
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
completely specific towards L-glutamate
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
a key enzyme in the bacterial pathway to L-lysine
-
-
-
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
show the reaction diagram
Q8NRE6
-
-
-
?
additional information
?
-
-
structural requirements for substrate recognition
-
-
-
additional information
?
-
-
enzyme is not identical to N-acetylornithine aminotransferase
-
-
-
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
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
-
a key enzyme in the bacterial pathway to L-lysine
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
a pyridoxal phosphate protein
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
O53870
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-(N-(succinylamino))-6-hydrazinoheptane-1,7-dioic acid
-
very potent slow-binding inhibitor, synthesis
2-(N-Carbobenzoxy-amino)-6-hydrazinoheptane-1,7-dioic acid
-
very potent slow-binding inhibitor, synthesis
2-oxoglutarate
-
at high concentrations, inhibition in both directions
carbenicillin
-
-
Chloramphenicol
-
-
tetracycline
-
-
hydroxylamine
-
-
additional information
-
synthesis of hydrazino product analogues which are potent slow tight-binding inhibitors, kinetics
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.21
-
L-glutamate
-
30C, pH 8.0
5.2
-
L-glutamate
-
pH 7.4
0.18
-
N-Succinyl-2-amino-6-oxoheptanedioate
-
30C, pH 8.0
0.5
-
N-Succinyl-2-amino-6-oxoheptanedioate
-
pH 7.4
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000004
-
2-(N-(succinylamino))-6-hydrazinoheptane-1,7-dioic acid
-
30C, pH 8.0
0.000054
-
2-(N-Carbobenzoxy-amino)-6-hydrazinoheptane-1,7-dioic acid
-
30C, pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.33
-
-
pH 7.4
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
assay at
8
-
Q8NRE6
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9
-
pH 6.5: about 25% of maximum activity, pH 9: about 60% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
Q8NRE6
assay at
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
82000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 39900, SDS-PAGE, MALDI-TOF mass spectra
dimer
O53870
crystallization data
homodimer
O53870
x-ray crystallography
additional information
-
contains multiple imperfect-hexapeptide-repeat units
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
diffration to 2.0 A resolution. The orthorhombic crystals contain one functional dimer in the asymmetric unit. The homodimer displays the typical S-shape of class I pyridoxal 5'-phosphate-binding proteins. The two active sites of the dimer both feature an internal aldimine with the co-factor pyridoxal 5'-phosphate covalently bound to the Lys232, although neither substrate nor cofactor has been added during protein production, purification and crystallization. Nine water molecules are conserved in the active site and form an intricate hydrogen-bonding network with the co-factor and the surrounding amino acid residues; sitting drop vapour diffusion method, in the presence of 20% (w/v) PEG-3350, Tris-HCl (pH 8.5) and 200 mM MgCl2
O53870
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
affinity column chromatography and gel filtration
O53870
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
O53870
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
Q8NRE6
enzyme deletion mutant, normal growth with excess carbon and limited ammonium medium
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
Q8NRE6
overexpression of enzyme, increase in production of L-lysine, 10fold increase in enzyme activity of strain