EC 4.1.2.42 - D-threonine aldolase

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IntEnz Enzyme Nomenclature
EC 4.1.2.42

Names

Accepted name:
D-threonine aldolase
Other names:
D-TA
DTA
low specificity D-TA
low specificity D-threonine aldolase
Systematic name:
D-threonine acetaldehyde-lyase (glycine-forming)

Reactions

Cofactor

Comments:

A pyridoxal-phosphate protein that is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+) [1,2]. The reaction is reversible, which can lead to the interconversion of D-threonine and D-allothreonine [1]. Several other D-β-hydroxy-α-amino acids, such as D-β-phenylserine, D-β-hydroxy-α-aminovaleric acid and D-β-3,4-dihydroxyphenylserine, can also act as substrate [1].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0043876
UniProtKB/Swiss-Prot:

References

  1. Kataoka, M., Ikemi, M., Morikawa, T., Miyoshi, T., Nishi, K., Wada, M., Yamada, H. and Shimizu, S.
    Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38.
    Eur. J. Biochem. 248: 385-393 (1997). [PMID: 9346293]
  2. Liu, J.-Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H.
    A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization.
    J. Biol. Chem. 273: 16678-16685 (1998). [PMID: 9642221]
  3. Liu, J.Q., Odani, M., Dairi, T., Itoh, N., Shimizu, S. and Yamada, H.
    A new route to L-threo-3-[4-(methylthio)phenylserine], a key intermediate for the synthesis of antibiotics: recombinant low-specificity D-threonine aldolase-catalyzed stereospecific resolution.
    Appl. Microbiol. Biotechnol. 51: 586-591 (1999). [PMID: 10390816]
  4. Liu, J.Q., Odani, M., Yasuoka, T., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H.
    Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug.
    Appl. Microbiol. Biotechnol. 54: 44-51 (2000). [PMID: 10952004]
  5. Liu, J.-Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H.
    Diversity of microbial threonine aldolases and their application.
    J. Mol. Catal. B 10: 107-115 (2000).
  6. Paiardini, A., Contestabile, R., D'Aguanno, S., Pascarella, S. and Bossa, F.
    Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes.
    Biochim. Biophys. Acta 1647: 214-219 (2003). [PMID: 12686135]

[EC 4.1.2.42 created 2007]