D-threonine aldolase

D-threonine aldolase (EC 4.1.2.42, D-TA, DTA, low specificity D-TA, low specificity D-threonine aldolase) is an enzyme with systematic name D-threonine acetaldehyde-lyase (glycine-forming).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

(1) D-threonine glycine + acetaldehyde
(2) D-allothreonine glycine + acetaldehyde
D-threonine aldolase
Identifiers
EC no.4.1.2.42
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

This pyridoxal-phosphate protein is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+).

References
  1. Kataoka M, Ikemi M, Morikawa T, Miyoshi T, Nishi K, Wada M, Yamada H, Shimizu S (September 1997). "Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38". European Journal of Biochemistry. 248 (2): 385–93. doi:10.1111/j.1432-1033.1997.00385.x. PMID 9346293.
  2. Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (July 1998). "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". The Journal of Biological Chemistry. 273 (27): 16678–85. doi:10.1074/jbc.273.27.16678. PMID 9642221.
  3. Liu JQ, Odani M, Dairi T, Itoh N, Shimizu S, Yamada H (May 1999). "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". Applied Microbiology and Biotechnology. 51 (5): 586–91. doi:10.1007/s002530051436. PMID 10390816. S2CID 510986.
  4. Liu JQ, Odani M, Yasuoka T, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (July 2000). "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". Applied Microbiology and Biotechnology. 54 (1): 44–51. doi:10.1007/s002539900301. PMID 10952004. S2CID 23861506.
  5. Liu, J.Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H. (2000). "Diversity of microbial threonine aldolases and their application". J. Mol. Catal. B. 10 (1–3): 107–115. doi:10.1016/s1381-1177(00)00118-1.
  6. Paiardini A, Contestabile R, D'Aguanno S, Pascarella S, Bossa F (April 2003). "Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1647 (1–2): 214–9. doi:10.1016/s1570-9639(03)00050-5. PMID 12686135.


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