Low-specificity L-threonine aldolase

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Low-specificity L-threonine aldolase
Identifiers
EC number 4.1.2.48
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB 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 glycine + acetaldehyde
(2) L-allo-threonine glycine + acetaldehyde

This enzyme requires pyridoxal phosphate.

References[edit]

  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. 

External links[edit]