Information on EC 2.6.1.17 - succinyldiaminopimelate transaminase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.6.1.17
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RECOMMENDED NAME
GeneOntology No.
succinyldiaminopimelate transaminase
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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
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine biosynthesis I
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-
lysine metabolism
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Lysine biosynthesis
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-
Metabolic pathways
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Microbial metabolism in diverse environments
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-
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SYSTEMATIC NAME
IUBMB Comments
N-succinyl-L-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-46-0
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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-
-
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.
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-
-
Manually annotated by BRENDA team
no activity in Sus scrofa
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-
-
Manually annotated by BRENDA team
bifunctional diaminopimelate aminotransferase and aspartate:prephenate aminotransferase, EC 2.6.1.79
UniProt
Manually annotated by BRENDA team
bifunctional diaminopimelate aminotransferase and aspartate:prephenate aminotransferase, EC 2.6.1.79
UniProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
in Escherichia coli, the major enzymes with N-succinyl-L,L-diaminopimelate aminotransferase (SDAP-AT) activity in lysine synthesis are ArgD, AstC, and SerC. Lysine availability does not regulate synthesis of the major SDAP-ATs. Complementation analysis of mutants lacking aminotransferases shows that the SDAP-ATs and alanine aminotransferases are exceptionally redundant, and this redundancy may ensure peptidoglycan synthesis
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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
-
-
-
?
prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
show the reaction diagram
additional information
?
-
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
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2-(N-(succinylamino))-6-hydrazinoheptane-1,7-dioic acid
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very potent slow-binding inhibitor, synthesis
2-(N-Carbobenzoxy-amino)-6-hydrazinoheptane-1,7-dioic acid
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very potent slow-binding inhibitor, synthesis
2-oxoglutarate
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at high concentrations, inhibition in both directions
carbenicillin
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Chloramphenicol
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hydroxylamine
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tetracycline
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-
additional information
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synthesis of hydrazino product analogues which are potent slow tight-binding inhibitors, kinetics
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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
0.021
prephenate
pH 8.0, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24
prephenate
pH 8.0, 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000004
2-(N-(succinylamino))-6-hydrazinoheptane-1,7-dioic acid
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30°C, pH 8.0
0.000054
2-(N-Carbobenzoxy-amino)-6-hydrazinoheptane-1,7-dioic acid
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30°C, pH 8.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.33
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pH 7.4
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
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pH 6.5: about 25% of maximum activity, pH 9: about 60% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39900
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2 * 39900, SDS-PAGE, MALDI-TOF mass spectra
82000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
additional information
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contains multiple imperfect-hexapeptide-repeat units
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity column chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
enzyme deletion mutant, normal growth with excess carbon and limited ammonium medium
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
overexpression of enzyme, increase in production of L-lysine, 10fold increase in enzyme activity of strain
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Show AA Sequence (2335 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.6.1.17)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)