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-allo-threonine
glycine + acetaldehyde
This enzyme requires pyridoxal phosphate.
References
- ↑ 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.
- ↑ 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.
- ↑ 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 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.
- ↑ 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.
- ↑ 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.
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