|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Mass balance status: Balanced.
Direct generic reaction:
DL-allothreonine → acetaldehyde + glycine (4.1.2.-)
Enzyme Commission Primary Name for 18.104.22.168: low-specificity L-threonine aldolase
Enzyme Commission Synonyms for 22.214.171.124: LtaE
Enzyme Commission Primary Name for 126.96.36.199: L-allo-threonine aldolase
Enzyme Commission Summary for 188.8.131.52:
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 [Liu97]. Different from EC 184.108.40.206, L-threonine aldolase, and EC 220.127.116.11, L-allo-threonine aldolase.
Enzyme Commission Summary for 18.104.22.168:
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 22.214.171.124, L-threonine aldolase, and EC 126.96.36.199, low-specificity L-threonine aldolase. A previously listed enzyme with this name, EC 188.8.131.52, was deleted in 1971 after it was found to be identical to EC 184.108.40.206, glycine hydroxymethyltransferase.
Kataoka97: 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
Kim10c: 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
Liu97: 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
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