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|
| |
4.1.2.5 |
| Activity |
4.1.2.5 |
| Description |
Threonine aldolase. |
| Notes |
Heterogeneous family, strictly related to fungal alanine racemases (family 5.1.1.1_b) and to phenylserine aldolases (family 4.1.2.26).
Indeed, many of the characterized bacterial enzymes can also carry out the phenylserine aldolase reaction.
Part of the heterogeneity of the family can be attributed to differences in substrate speciticity. In fact, L-threonine aldolases can be subdivided into three sub-types: L-specific threonine aldolases, which preferably cleave L-threonine; l-allo-threonine aldolase, which cleave l-allo-threonine; and low specificity threonine aldolases, that accept both l-Thr and l-allo-Thr as substrates. |
| PDB |
1JG8; |
| PLP Fold Type |
I |
| PLP-dependent Domain |
|
| Number of sequences |
40 |
| Sequences in seed alignment |
|
| Reference sequence |
LTAE_ECOLI |
| Domain interval |
3-286 |
| Catalytic site |
197 K |
| | |
|---|
| References |
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.. |
| last changed |
2008/02/05 17:43 |
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