Low-specificity L-threonine aldolase
Low-specificity L-threonine aldolase | |||||||||
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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 | ||||||||
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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.; 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.; 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.; 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.; 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.; 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 3010111. PMID 21119630.
External links
- Low-specificity L-threonine aldolase at the US National Library of Medicine Medical Subject Headings (MeSH)
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