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 reactions:
| Low-specificity L-threonine aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 | ||||||||
| |||||||||
- L-threonine glycine acetaldehyde
- L-allothreonine glycine acetaldehyde
This enzyme requires pyridoxal phosphate.
References
edit- ^ Yamada H, Kumagai H, Nagate T, Yoshida H (April 1970). "Crystalline threonine aldolase from Candida humicola". Biochemical and Biophysical Research Communications. 39 (1): 53–8. doi:10.1016/0006-291x(70)90756-4. PMID 5438301.53-8&rft.date=1970-04&rft_id=info:doi/10.1016/0006-291x(70)90756-4&rft_id=info:pmid/5438301&rft.aulast=Yamada&rft.aufirst=H&rft.au=Kumagai, H&rft.au=Nagate, T&rft.au=Yoshida, H&rfr_id=info:sid/en.wikipedia.org:Low-specificity L-threonine aldolase" class="Z3988">
- ^ Kumagai H, Nagate T, Yoshida H, Yamada H (March 1972). "Threonine aldolase from Candida humicola. II. Purification, crystallization and properties". Biochimica et Biophysica Acta (BBA) - Enzymology. 258 (3): 779–90. doi:10.1016/0005-2744(72)90179-9. PMID 5017702.779-90&rft.date=1972-03&rft_id=info:doi/10.1016/0005-2744(72)90179-9&rft_id=info:pmid/5017702&rft.aulast=Kumagai&rft.aufirst=H&rft.au=Nagate, T&rft.au=Yoshida, H&rft.au=Yamada, H&rfr_id=info:sid/en.wikipedia.org:Low-specificity L-threonine aldolase" class="Z3988">
- ^ Liu JQ, Nagata S, Dairi T, Misono H, Shimizu S, Yamada H (April 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". European Journal of Biochemistry. 245 (2): 289–93. doi:10.1111/j.1432-1033.1997.00289.x. PMID 9151955.289-93&rft.date=1997-04&rft_id=info:doi/10.1111/j.1432-1033.1997.00289.x&rft_id=info:pmid/9151955&rft.aulast=Liu&rft.aufirst=JQ&rft.au=Nagata, S&rft.au=Dairi, T&rft.au=Misono, H&rft.au=Shimizu, S&rft.au=Yamada, H&rft_id=https://doi.org/10.1111%2Fj.1432-1033.1997.00289.x&rfr_id=info:sid/en.wikipedia.org:Low-specificity L-threonine aldolase" class="Z3988">
- ^ Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (July 1998). "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. doi:10.1046/j.1432-1327.1998.2550220.x. PMID 9692922.220-6&rft.date=1998-07&rft_id=info:doi/10.1046/j.1432-1327.1998.2550220.x&rft_id=info:pmid/9692922&rft.aulast=Liu&rft.aufirst=JQ&rft.au=Dairi, T&rft.au=Itoh, N&rft.au=Kataoka, M&rft.au=Shimizu, S&rft.au=Yamada, H&rft_id=https://doi.org/10.1046%2Fj.1432-1327.1998.2550220.x&rfr_id=info:sid/en.wikipedia.org:Low-specificity L-threonine aldolase" class="Z3988">
- ^ Kim J, Kershner JP, Novikov Y, Shoemaker RK, Copley SD (November 2010). "Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis". Molecular Systems Biology. 6: 436. doi:10.1038/msb.2010.88. PMC 3010111. PMID 21119630.
External links
edit- Low-specificity L-threonine aldolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
