|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Direct generic reaction:
DL-allothreonine ↔ acetaldehyde + glycine (4.1.2.-)
Enzyme Commission Primary Name for 184.108.40.206: low-specificity L-threonine aldolase
Enzyme Commission Synonyms for 220.127.116.11: LtaE
Enzyme Commission Primary Name for 18.104.22.168: L-allo-threonine aldolase
Enzyme Commission Summary for 22.214.171.124:
Requires pyridoxal phosphate. The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine [Yamada70, Kumagai72]. The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine [Liu98]. The enzyme can also catalyse the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis [Liu97a]. Different from EC 126.96.36.199, L-threonine aldolase, and EC 188.8.131.52, L-allo-threonine aldolase.
Enzyme Commission Summary for 184.108.40.206:
Requires pyridoxal phosphate. This enzyme, characterized from the bacterium Aeromonas jandaei, is specific for L-allo-threonine and can not act on either L-threonine or L-serine. Different from EC 220.127.116.11, L-threonine aldolase, and EC 18.104.22.168, low-specificity L-threonine aldolase. A previously listed enzyme with this name, EC 22.214.171.124, was deleted in 1971 after it was found to be identical to EC 126.96.36.199, glycine hydroxymethyltransferase.
Instance reaction of [DL-allothreonine ↔ acetaldehyde + glycine] (4.1.2.-):
i1: L-allo-threonine ↔ glycine + acetaldehyde (188.8.131.52/184.108.40.206)
Kataoka97a: Kataoka M, Wada M, Nishi K, Yamada H, Shimizu S (1997). "Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39." FEMS Microbiol Lett 151(2);245-8. PMID: 9228760
Kim10a: Kim J, Kershner JP, Novikov Y, Shoemaker RK, Copley SD (2010). "Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis." Mol Syst Biol 6;436. PMID: 21119630
Kumagai72: Kumagai H, Nagate T, Yoshida H, Yamada H (1972). "Threonine aldolase from Candida humicola. II. Purification, crystallization and properties." Biochim Biophys Acta 258(3);779-90. PMID: 5017702
Liu97a: Liu JQ, 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(2);289-93. PMID: 9151955
Liu98: Liu JQ, 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 1998;255(1);220-6. PMID: 9692922
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493