View source for Low-specificity L-threonine aldolase

{{Infobox enzyme
| Name       = Low-specificity <small>L</small>-threonine aldolase
| EC_number  = 4.1.2.48
| CAS_number =
| GO_code    = 
| image      = 
| width      = 
| caption    =  
}}
'''Low-specificity <small>L</small>-threonine aldolase''' ({{EnzExplorer|4.1.2.48}}, ''LtaE'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''<small>L</small>-threonine/<small>L</small>-allo-threonine acetaldehyde-lyase (glycine-forming)''.<ref>{{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 }}</ref><ref>{{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 }}</ref><ref>{{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 <small>L</small>-threonine aldolase that catalyzes cleavage of <small>L</small>-''allo''-threonine and <small>L</small>-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 }}</ref><ref>{{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 <small>L</small>-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 }}</ref><ref>{{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 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]s:

:<small>L</small>-[[threonine]] <math>\rightleftharpoons</math> [[glycine]] + [[acetaldehyde]]
:<small>L</small>-[[allothreonine]] <math>\rightleftharpoons</math> glycine + acetaldehyde

This enzyme requires pyridoxal phosphate.

== References ==
{{reflist}}

== External links ==
* {{MeshName|Low-specificity+L-threonine+aldolase}}

{{Carbon-carbon lyases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}

[[Category:EC 4.1.2]]