EC 4.3.3.7 - 4-hydroxy-tetrahydrodipicolinate synthase

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IntEnz Enzyme Nomenclature
EC 4.3.3.7

Names

Accepted name:
4-hydroxy-tetrahydrodipicolinate synthase
Other names:
dihydrodipicolinic acid synthase [incorrect]
dihydropicolinate synthetase [incorrect]
dihydrodipicolinate synthetase [incorrect]
DHDPS
L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing)
dapA (gene name)
Systematic name:
L-aspartate-4-semialdehyde hydro-lyase [adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming]

Reaction

Comments:

The reaction can be divided into three consecutive steps: Schiff base formation with pyruvate, the addition of L-aspartate-semialdehyde, and finally transimination leading to cyclization with simultaneous dissociation of the product. The product of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate [1,2], and the enzyme was classified accordingly as EC 4.2.1.52, dihydrodipicolinate synthase. Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual product of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate [3], and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate synthase. However, the identity of the product is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all [5].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00569
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008840
UniProtKB/Swiss-Prot: (478) [show] [UniProt]

References

  1. Yugari, Y. and Gilvarg, C.
    The condensation step in diaminopimelate synthesis.
    J. Biol. Chem. 240: 4710-4716 (1965). [PMID: 5321309]
  2. Blickling, S., Renner, C., Laber, B., Pohlenz, H. D., Holak, T. A., Huber, R.
    Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy.
    Biochemistry 36: 24-33 (1997). [PMID: 8993314]
  3. 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]
  4. Soares da Costa, T. P., Muscroft-Taylor, A. C., Dobson, R. C., Devenish, S. R., Jameson, G. B., Gerrard, J. A.
    How essential is the 'essential' active-site lysine in dihydrodipicolinate synthase?
    Biochimie 92: 837-845 (2010). [PMID: 20353808]
  5. Salganicoff, L., Sevy, R. W.
    The platelet strip. II. Pharmacomechanical coupling in thrombin-activated human platelets.
    Am. J. Physiol. 249: C288-C296 (1985). [PMID: 2994486]

[EC 4.3.3.7 created 1972 as EC 4.2.1.52, transferred 2012 to EC 4.3.3.7]