:Low-specificity L-threonine aldolase

{{Infobox enzyme

| Name = Low-specificity L-threonine aldolase

| EC_number = 4.1.2.48

| CAS_number =

| GO_code =

| image =

| width =

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Low-specificity L-threonine aldolase ({{EnzExplorer|4.1.2.48}}, LtaE) is an enzyme with systematic name L-threonine/L-allo-threonine acetaldehyde-lyase (glycine-forming).{{cite journal | vauthors = Yamada H, Kumagai H, Nagate T, Yoshida H | title = Crystalline threonine aldolase from Candida humicola | journal = Biochemical and Biophysical Research Communications | volume = 39 | issue = 1 | pages = 53–8 | date = April 1970 | pmid = 5438301 | doi = 10.1016/0006-291x(70)90756-4 }}{{cite journal | vauthors = Kumagai H, Nagate T, Yoshida H, Yamada H | title = Threonine aldolase from Candida humicola. II. Purification, crystallization and properties | journal = Biochimica et Biophysica Acta (BBA) - Enzymology | volume = 258 | issue = 3 | pages = 779–90 | date = March 1972 | pmid = 5017702 | doi = 10.1016/0005-2744(72)90179-9 }}{{cite journal | vauthors = Liu JQ, Nagata S, Dairi T, Misono H, Shimizu S, Yamada H | title = 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 | journal = European Journal of Biochemistry | volume = 245 | issue = 2 | pages = 289–93 | date = April 1997 | pmid = 9151955 | doi = 10.1111/j.1432-1033.1997.00289.x | doi-access = free }}{{cite journal | vauthors = Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H | title = Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli | journal = European Journal of Biochemistry | volume = 255 | issue = 1 | pages = 220–6 | date = July 1998 | pmid = 9692922 | doi = 10.1046/j.1432-1327.1998.2550220.x | doi-access = free }}{{cite journal | vauthors = Kim J, Kershner JP, Novikov Y, Shoemaker RK, Copley SD | title = Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis | journal = Molecular Systems Biology | volume = 6 | pages = 436 | date = November 2010 | pmid = 21119630 | pmc = 3010111 | doi = 10.1038/msb.2010.88 }} This enzyme catalyses the following chemical reactions:

:L-threonine $\backslash rightleftharpoons$ glycine + acetaldehyde

:L-allothreonine $\backslash rightleftharpoons$ glycine + acetaldehyde

This enzyme requires pyridoxal phosphate.