Low-specificity L-threonine aldolase

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 \rightleftharpoons glycine + acetaldehyde
(2) L-allo-threonine \rightleftharpoons glycine + acetaldehyde

This enzyme requires pyridoxal phosphate.

References

  1. Yamada, H., Kumagai, H., Nagate, T. and 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. and 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. and 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 glycineexpression 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. and 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. and 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. PMID 21119630.

External links

This article is issued from Wikipedia - version of the Thursday, March 31, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.