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Description Threonine aldolase
Alternative names L-Threonine aldolase;
L-threonine acetaldehyde-lyase.
Catalyzed reaction L-threonine = glycine + acetaldehyde.
Cofactor Pyridoxal-phosphate.
Threonine aldolase is responsible of one of the three pathways of L-threonine degradation in bacteria, fungi and plants.
The importance of this pathway is marginal in metazoa, and some animals seem to completely lack the activity.

L-threonine aldolases can be subdivided into three sub-types: L-specific threonine aldolase (LTA), which preferably cleaves plain L-threonine; L-allo-threonine aldolase (LalloTA), which cleaves L-allo-threonine; and low specificity threonine aldolase (LlowTA) which accepts both L-Thr and L-allo-Thr as substrates.

Organisms -Eubacteria -Archea -Fungi -Metazoa

Family (41)
Links Enzyme (activities)
BRENDA (activities)
KEGG (pathways)
PLPMDB (PLP mutants)
 Fesko, K.; Reisinger, C.; Steinreiber, J.; Weber, H.; Schürmann. M.; Griengl, H. (2008) Four types of threonine aldolases: Similarities and differences in kinetics/thermodynamics J Mol Catal B: Enzymatic 52 19-26.

 Edgar, A.J. (2005) Mice have a transcribed L-threonine aldolase/GLY1 gene, but the human GLY1 gene is a non-processed pseudogene BMC Genomics 6 32.

 Jander G, Norris SR, Joshi V, Fraga M, Rugg A, Yu S, Li L, Last R.L. (2004) Application of a high-throughput HPLC-MS/MS assay to Arabidopsis mutant screening; evidence that threonine aldolase plays a role in seed nutritional quality Plant J 39 465-75.

 Kielkopf, C. L.; Burley, S. K. (2002) X-ray structures of threonine aldolase complexes: Structural basis of substrate recognition Biochemistry 41 11711-20.

 McNeil JB, Flynn J, Tsao N, Monschau N, Stahmann K, Haynes RH, McIntosh EM, Pearlman RE. (2000) Glycine metabolism in Candida albicans: characterization of the serine hydroxymethyltransferase (SHM1, SHM2) and threonine aldolase (GLY1) genes Yeast 16 167-75.

 Liu, J. Q.; 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 255 220-6.

 Liu, J. Q.; Ito, S.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H. (1998) Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558 Appl Environ Microbiol 64 549-54.

 Liu, J. Q.; Dairi, T.; Kataoka, M.; Shimizu, S.; Yamada, H. (1997) L-allo-threonine aldolase from Aeromonas jandaei DK-39: gene cloning, nucleotide sequencing, and identification of the pyridoxal 5'-phosphate- binding lysine residue by site-directed mutagenesis J Bacteriol 179 3555-60.

 Liu, J. Q.; 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 245 289-93.

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last changed 2019/06/20 11:24

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