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
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
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine biosynthesis I
-
-
Lysine biosynthesis
-
-
lysine metabolism
-
-
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
COMMENTARY
LITERATURE
aminotransferase, succinyldiaminopimelate
-
-
-
-
DAP-AT
-
-
-
-
N-succinyl-L-diaminopimelic-glutamic transaminase
-
-
-
-
succinyldiaminopimelate aminotransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9030-46-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
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
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
P9WPZ5
-
-
-
?
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
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
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
a pyridoxal phosphate protein
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
P9WPZ5
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
-
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]
SUBSTRATE
ORGANISM
UNIPROT
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]
INHIBITOR
ORGANISM
UNIPROT
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]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.33
-
pH 7.4
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
pH 6.5: about 25% of maximum activity, pH 9: about 60% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Q8NRE6
assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
82000
-
gel filtration
636967
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
P9WPZ5
crystallization data
dimer
-
2 * 39900, SDS-PAGE, MALDI-TOF mass spectra
homodimer
P9WPZ5
x-ray crystallography
additional information
-
contains multiple imperfect-hexapeptide-repeat units
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
P9WPZ5
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity column chromatography and gel filtration
P9WPZ5
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
P9WPZ5
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Q8NRE6
enzyme deletion mutant, normal growth with excess carbon and limited ammonium medium
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
Q8NRE6
overexpression of enzyme, increase in production of L-lysine, 10fold increase in enzyme activity of strain