Information on EC 2.6.1.17 - succinyldiaminopimelate transaminase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
2.6.1.17
-
RECOMMENDED NAME
GeneOntology No.
succinyldiaminopimelate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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 hide
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-46-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-L-2,6-diaminoheptanedioate + 2-oxoglutarate
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
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
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
hydroxylamine
-
-
tetracycline
-
-
additional information
-
synthesis of hydrazino product analogues which are potent slow tight-binding inhibitors, kinetics
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.21 - 5.2
L-glutamate
0.18 - 0.5
N-Succinyl-2-amino-6-oxoheptanedioate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
5.33
-
pH 7.4
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
pH 6.5: about 25% of maximum activity, pH 9: about 60% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
82000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity column chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
enzyme deletion mutant, normal growth with excess carbon and limited ammonium medium
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
overexpression of enzyme, increase in production of L-lysine, 10fold increase in enzyme activity of strain
Show AA Sequence (2703 entries)
Please use the Sequence Search for a certain query.