The Enzyme Database

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Accepted name: D-threonine aldolase
Reaction: (1) D-threonine = glycine + acetaldehyde
(2) D-allo-threonine = glycine + acetaldehyde
Glossary: D-threonine = (2R,3S)-2-amino-3-hydroxybutanoic acid
D-allothreonine = (2R,3R)-2-amino-3-hydroxybutanoic acid
Other name(s): D-TA; DTA; low specificity D-TA; low specificity D-threonine aldolase
Systematic name: D-threonine acetaldehyde-lyase (glycine-forming)
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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 (1997) 385–393. [DOI] [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 (1998) 16678–16685. [DOI] [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 (1999) 586–591. [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 (2000) 44–51. [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 (2000) 107–115.
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 (2003) 214–219. [DOI] [PMID: 12686135]
[EC created 2007]

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