Low-specificity L-threonine aldolase

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Low-specificity L-threonine aldolase
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Low-specificity L-threonine aldolase (EC, LtaE) is an enzyme with systematic name L-threonine/L-allo-threonine acetaldehyde-lyase (glycine-forming).[1][2][3][4][5] This enzyme catalyses the following chemical reaction

(1) L-threonine glycine + acetaldehyde
(2) L-allo-threonine glycine + acetaldehyde

This enzyme requires pyridoxal phosphate.


  1. ^ Yamada, H.; Kumagai, H.; Nagate, T.; Yoshida, H. (1970). "Crystalline threonine aldolase from Candida humicola". Biochem. Biophys. Res. Commun. 39: 53–58. doi:10.1016/0006-291x(70)90756-4. PMID 5438301. 
  2. ^ Kumagai, H.; Nagate, T.; Yoshida, H.; Yamada, H. (1972). "Threonine aldolase from Candida humicola. II. Purification, crystallization and properties". Biochim. Biophys. Acta. 258: 779–790. doi:10.1016/0005-2744(72)90179-9. PMID 5017702. 
  3. ^ Liu, J.Q.; Nagata, S.; Dairi, T.; Misono, H.; Shimizu, S.; Yamada, H. (1997). "The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine—expression of the gene in Escherichia coli and purification and characterization of the enzyme". Eur. J. Biochem. 245: 289–293. doi:10.1111/j.1432-1033.1997.00289.x. PMID 9151955. 
  4. ^ Liu, J.Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H. (1998). "Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli". Eur. J. Biochem. 255: 220–226. doi:10.1046/j.1432-1327.1998.2550220.x. PMID 9692922. 
  5. ^ Kim, J.; Kershner, J.P.; Novikov, Y.; Shoemaker, R.K.; Copley, S.D. (2010). "Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5′-phosphate synthesis". Mol. Syst. Biol. 6: #436–436. doi:10.1038/msb.2010.88. PMC 3010111Freely accessible. PMID 21119630. 

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