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Information on EC 2.6.1.17 - succinyldiaminopimelate transaminase
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2.6.1.17 succinyldiaminopimelate transaminaseIUBMB Comments
A pyridoxal-phosphate protein.
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The enzyme appears in viruses and cellular organisms
Synonyms
aminotransferase, succinyldiaminopimelate, AspB2, DAP-AT, DapC, N-succinyl-L-diaminopimelic-glutamic transaminase, Rv0858c, SDAT-AT, succinyldiaminopimelate aminotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminotransferase, succinyldiaminopimelate
-
-
-
-
AspB2
DAP-AT
DapC
N-succinyl-L-diaminopimelic-glutamic transaminase
-
-
-
-
succinyldiaminopimelate aminotransferase
-
-
-
-
DAP-AT
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-L-2-amino-6-oxoheptanedioate + L-glutamate
A pyridoxal-phosphate protein
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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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
9030-46-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
-
-
-
?
prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
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
-
completely specific towards L-glutamate
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
a key enzyme in the bacterial pathway to L-lysine
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
?
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
r
prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
-
-
-
?
prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
-
-
-
?
additional information
?
-
-
structural requirements for substrate recognition
-
-
-
additional information
?
-
-
enzyme is not identical to N-acetylornithine aminotransferase
-
-
-
additional information
?
-
-
enzyme is not identical to N-acetylornithine aminotransferase
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
a key enzyme in the bacterial pathway to L-lysine
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
-
-
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
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
additional information
-
synthesis of hydrazino product analogues which are potent slow tight-binding inhibitors, kinetics
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000004
2-(N-(succinylamino))-6-hydrazinoheptane-1,7-dioic acid
-
30°C, pH 8.0
0.000054
2-(N-Carbobenzoxy-amino)-6-hydrazinoheptane-1,7-dioic acid
-
30°C, pH 8.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
pH 6.5: about 25% of maximum activity, pH 9: about 60% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional diaminopimelate aminotransferase and aspartate:prephenate aminotransferase, EC 2.6.1.79
UniProt
brenda
bifunctional diaminopimelate aminotransferase and aspartate:prephenate aminotransferase, EC 2.6.1.79
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
Show AA Sequence and Transmembrane Helices (4914 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Aspergillus kawachii (strain NBRC 4308)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
-
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
enzyme deletion mutant, normal growth with excess carbon and limited ammonium medium
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
overexpression of enzyme, increase in production of L-lysine, 10fold increase in enzyme activity of strain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vaara, M.
Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme
FEMS Microbiol. Lett.
97
249-254
1992
Escherichia coli
-
brenda
Peterkofsky, B.; Gilvarg, C.
N-succinyl-L-diaminopimelic-glutamic transaminase
J. Biol. Chem.
236
1432-1438
1961
Alcaligenes faecalis, Azotobacter vinelandii, Desmonostoc muscorum, Escherichia coli, Klebsiella aerogenes, Lactobacillus plantarum, Micrococcus luteus, no activity in Brewer's yeast, no activity in Lactobacillus casei, no activity in Streptococcus sp., no activity in Sus scrofa, Rhodobacter sphaeroides
brenda
Cox, R.J.; Sherwin, W.A.; Lam, L.K.P.; Vederas, J.C.
Synthesis and evaluation of novel substrates and inhibitors of N-succinyl-LL-diaminopimelate aminotransferase (DAP-AT) from Escherichia coli
J. Am. Chem. Soc.
118
7449-7460
1996
Escherichia coli
-
brenda
Cox, R.J.; Schouten, J.A.; Stentiford, R.A.; Wareing, K.J.
Peptide inhibitors of N-succinyl diaminopimelic acid aminotransferase (DAP-AT): a novel class of antimicrobial compounds
Bioorg. Med. Chem. Lett.
8
945-950
1998
Escherichia coli
brenda
Cox, R.J.; Wang, P.S.H.
Is N-acetylornithine aminotransferase the real N-succinyl-LL-diaminopimelate aminotransferase in Escherichia coli and Mycobacterium smegmatis?
J. Chem. Soc. Perkin Trans. I
1
2006-2008
2001
Escherichia coli, Mycolicibacterium smegmatis
-
brenda
Fuchs, T.M.; Schneider, B.; Krumbach, K.; Eggeling, L.; Gross, R.
Characterization of a Bordetella pertussis diaminopimelate (DAP) biosynthesis locus identifies dapC, a novel gene coding for an N-succinyl-L,L-DAP aminotransferase
J. Bacteriol.
182
3626-3631
2000
Bordetella pertussis (Q9ZEX3)
brenda
Hartmann, M.; Tauch, A.; Eggeling, L.; Bathe, B.; Mockel, B.; Puhler, A.; Kalinowski, J.
Identification and characterization of the last two unknown genes, dapC and dapF, in the succinylase branch of the L-lysine biosynthesis of Corynebacterium glutamicum
J. Biotechnol.
104
199-211
2003
Corynebacterium glutamicum (Q8NRE6)
brenda
Weyand, S.; Kefala, G.; Weiss, M.S.
The three-dimensional structure of N-succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis
J. Mol. Biol.
367
825-838
2007
Mycobacterium tuberculosis (P9WPZ5), Mycobacterium tuberculosis H37Rv (P9WPZ5)
brenda
Graindorge, M.; Giustini, C.; Kraut, A.; Moyet, L.; Curien, G.; Matringe, M.
Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms
J. Biol. Chem.
289
3198-3208
2014
Streptomyces avermitilis (Q82IK5), Streptomyces avermitilis DSM 46492 (Q82IK5)
brenda
Lal, P.B.; Schneider, B.L.; Vu, K.; Reitzer, L.
The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli
Mol. Microbiol.
94
843-856
2014
Escherichia coli
brenda
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