2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.3.1.117 | ||||||||
CAS no. | 88086-34-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (EC 2.3.1.117) is an enzyme that catalyzes the chemical reaction
- succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O CoA + N-succinyl-L-2-amino-6-oxoheptanedioate
The 3 substrates of this enzyme are succinyl-CoA, (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, and H2O, whereas its two products are CoA and N-succinyl-L-2-amino-6-oxoheptanedioate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is succinyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. Other names in common use include tetrahydropicolinate succinylase, tetrahydrodipicolinate N-succinyltransferase, tetrahydrodipicolinate succinyltransferase, succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase, succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, and N-succinyltransferase. This enzyme participates in lysine biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1KGQ, 1KGT, 2TDT, and 3TDT.
References
- Simms SA, Voige WH, Gilvarg C (1984). "Purification and characterization of succinyl-CoA: tetrahydrodipicolinate N-succinyltransferase from Escherichia coli". J. Biol. Chem. 259 (5): 2734–41. PMID 6365916.