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Ligand L-2-aminopimelate Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C7 H1 3 NO4
L-2-aminopimelate
JUQLUIFNNFIIKC-YFKPBYRVSA-L
L-2-Aminoheptane-1,7-dioate
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (5 results)
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succinyl-CoA + L-2-aminopimelate = CoA + N-succinyl-L-aminopimelate
succinyl-CoA + L-2-aminopimelate = CoA + N-succinyl-L-aminopimelate
succinyl-CoA + L-2-aminopimelate = CoA + N-succinyl-L-aminopimelate
succinyl-CoA + L-2-aminopimelate = CoA + N-succinyl-L-aminopimelate
L-2-aminoheptane-1,7-dioate + 2-oxoglutarate = 2-oxoheptane-1,7-dioate + L-glutamate
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3D Structure of Enzyme-Ligand-Complex (PDB) (8 results)
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Enzyme Kinetic Parameters
KM Value (1 result)
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References & Links Literature References (3)
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Studies on the active site of succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase. Characterization using analogs of tetrahydrodipicolinate
1986
Berges, D.A.; DeWolf, W.E.; Dunn, G.L.; Newmann, D.J.; Schmidt, S.J.; Taggart, J.J.; Gilvarg, C.
J. Biol. Chem.
261
6160-6167
Kynurenine-oxoglutarate aminotransferase from rat kidney
1987
Tobes, M.C.
Methods Enzymol.
142
217-224
Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding
2008
Nguyen, L.; Kozlov, G.; Gehring, K.
FEBS Lett.
582
623-626
Links to other databases for L-2-aminopimelate