Low-specificity L-threonine aldolase

Low-specificity L-threonine aldolase (EC 4.1.2.48, 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-allothreonine glycine + acetaldehyde
Low-specificity L-threonine aldolase
Identifiers
EC number4.1.2.48
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

This enzyme requires pyridoxal phosphate.

References
  1. Yamada H, Kumagai H, Nagate T, Yoshida H (April 1970). "Crystalline threonine aldolase from Candida humicola". Biochemical and Biophysical Research Communications. 39 (1): 53–8. doi:10.1016/0006-291x(70)90756-4. PMID 5438301.
  2. Kumagai H, Nagate T, Yoshida H, Yamada H (March 1972). "Threonine aldolase from Candida humicola. II. Purification, crystallization and properties". Biochimica et Biophysica Acta (BBA) - Enzymology. 258 (3): 779–90. doi:10.1016/0005-2744(72)90179-9. PMID 5017702.
  3. Liu JQ, Nagata S, Dairi T, Misono H, Shimizu S, Yamada H (April 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". European Journal of Biochemistry. 245 (2): 289–93. doi:10.1111/j.1432-1033.1997.00289.x. PMID 9151955.
  4. Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (July 1998). "Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli". European Journal of Biochemistry. 255 (1): 220–6. doi:10.1046/j.1432-1327.1998.2550220.x. PMID 9692922.
  5. Kim J, Kershner JP, Novikov Y, Shoemaker RK, Copley SD (November 2010). "Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis". Molecular Systems Biology. 6: 436. doi:10.1038/msb.2010.88. PMC 3010111. PMID 21119630.
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