CATH Classification
Domain Context
CATH Clusters
| Superfamily | Tetrahydrodipicolinate-N-succinyltransferase, N-terminal domain |
| Functional Family | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase |
Enzyme Information
| 2.3.1.117 |
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase.
based on mapping to UniProt Q8X8Y7
Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate.
-!- Involved in the biosynthesis of lysine in bacteria, cyanobacteria and higher plants. -!- Earlier erroneously called 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase.
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UniProtKB Entries (1)
| Q8X8Y7 |
DAPD_ECO57
Escherichia coli O157:H7
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
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PDB Structure
| PDB | 3BXY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding.
Febs Lett.
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