Threonine aldolase
| threonine aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| L-Threonine aldolase homotetramer, Thermotoga maritima | |||||||||
| Identifiers | |||||||||
| EC no. | 4.1.2.5 | ||||||||
| CAS no. | 62213-23-4 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme threonine aldolase (EC 4.1.2.5) is an enzyme not found in humans that catalyzes the chemical reaction
- L-threonine {\displaystyle \rightleftharpoons } glycine + acetaldehyde
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-threonine acetaldehyde-lyase (glycine-forming). This enzyme is also called L-threonine acetaldehyde-lyase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
[edit ]As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1JG8 , PDB: 1LW4 , PDB: 1LW5 , PDB: 1M6S , and PDB: 1SVV .
Presence in human and mouse
[edit ]| THA1P | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | THA1P , GLY1, threonine aldolase 1, pseudogene | |||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | GeneCards: THA1P | |||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | ||||||||||||||||||||||||||||||||||||||||||||||||||
Some early evidence from 2005 suggests that the mouse ortholog enzyme, Tha1 (or GLY1), is synthesized and functional in mice,[2] [3] but this has not been reviewed by certain major groups like UniProt (as of August 2026).[4]
Humans also have the remnants of the gene denoted THA1P (or GLY1),[3] however it seems to be damaged by past mutations and inactive.[2] RNA expression has not been found in major databases, suggesting that it isn't transcribed.[2] Moreover, the pseudogene contains two single nucleotide deletions which would cause frameshifts even if were to be transcribed.[2]
References
[edit ]- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- 1 2 3 4 Alasdair J Edgar (2005) Mice have a transcribed L-threonine aldolase/GLY1 gene, but the human GLY1 gene is a non-processed pseudogene. BMC Genomics March 2005, 6:32. pdf
- 1 2 "Tha1 threonine aldolase 1 [ Mus musculus (house mouse) ]". ncbi.nlm.nih.gov. Retrieved 2026年08月12日.
- ↑ "Q6XPS7 · Q6XPS7_MOUSE". uniprot.org. UniProt consortium. Retrieved 2026年08月12日.
- Bell SC; Turner JM (1973). "Bacterial threonine aldolase and serine hydroxymethyltransferase enzyme". Biochem. Soc. Trans. 1 (3): 678–681. doi:10.1042/bst0010678.
- KARASEK MA, GREENBERG DM (1957). "Studies on the properties of threonine aldolases". J. Biol. Chem. 227 (1): 191–205. doi:10.1016/S0021-9258(18)70806-5 . PMID 13449064.
- 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. doi:10.1016/0005-2744(72)90179-9. PMID 5017702.
