Biology:Low-specificity L-threonine aldolase

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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

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 [math]\displaystyle{ \rightleftharpoons }[/math] glycine + acetaldehyde
(2) L-allothreonine [math]\displaystyle{ \rightleftharpoons }[/math] glycine + acetaldehyde

This enzyme requires pyridoxal phosphate.

References

  1. "Crystalline threonine aldolase from Candida humicola". Biochemical and Biophysical Research Communications 39 (1): 53–8. April 1970. doi:10.1016/0006-291x(70)90756-4. PMID 5438301. 
  2. "Threonine aldolase from Candida humicola. II. Purification, crystallization and properties". Biochimica et Biophysica Acta (BBA) - Enzymology 258 (3): 779–90. March 1972. doi:10.1016/0005-2744(72)90179-9. PMID 5017702. 
  3. "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. April 1997. doi:10.1111/j.1432-1033.1997.00289.x. PMID 9151955. 
  4. "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. July 1998. doi:10.1046/j.1432-1327.1998.2550220.x. PMID 9692922. 
  5. "Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis". Molecular Systems Biology 6: 436. November 2010. doi:10.1038/msb.2010.88. PMID 21119630. 

External links