EC - 4-hydroxy-tetrahydrodipicolinate reductase

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IntEnz Enzyme Nomenclature


Accepted name:
4-hydroxy-tetrahydrodipicolinate reductase
Other names:
dihydrodipicolinic acid reductase [incorrect]
dihydrodipicolinate reductase [incorrect]
dapB (gene name)
2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase [incorrect]
Systematic name:
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate:NADP+ 4-oxidoreductase



The substrate of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate [1], and the enzyme was classified accordingly as EC, dihydrodipicolinate reductase. Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual substrate of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate, and that its activity includes a dehydration step [2], and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate reductase. However, the identity of the substrate is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC01000
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008839
UniProtKB/Swiss-Prot: (567) [show] [UniProt]


  1. Farkas, W. and Gilvarg, C.
    The reduction step in diaminopimelic acid biosynthesis.
    J. Biol. Chem. 240 : 4717-4722 (1965). [PMID: 4378965]
  2. Devenish, S. R., Blunt, J. W., Gerrard, J. A.
    NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase.
    J. Med. Chem. 53 : 4808-4812 (2010). [PMID: 20503968]
  3. Karsten, W. E., Nimmo, S. A., Liu, J., Chooback, L.
    Identification of 2, 3-dihydrodipicolinate as the product of the dihydrodipicolinate synthase reaction from Escherichia coli.
    Arch. Biochem. Biophys. 653 : 50-62 (2018). [PMID: 29944868]

[EC created 1976 as EC, transferred 2013 to EC]