EC number:4.1.2.5
| ID: | 4.1.2.5 |
|---|---|
| Description: | L-threonine aldolase. |
| Alternative Name: |
L-threonine acetaldehyde-lyase. |
| Cath: | 3.40.640.10; 3.90.1150.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.2.5 |
| BRENDA Enzyme Link: | BRENDA 4.1.2.5 |
| KEGG Enzyme Link: | KEGG4.1.2.5 |
| BioCyc Enzyme Link: | BioCyc 4.1.2.5 |
| ExPASy Enzyme Link: | ExPASy4.1.2.5 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.2.5 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.2.5 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.2.5 |
| IntEnz Enzyme Link: | IntEnz 4.1.2.5 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.2.5 |
| RHEA:19625 | L-threonine = acetaldehyde + glycine |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[CH2;+0:2]-[*:3].[*:5]-[CH;+0:4]=[O;H0;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli. | Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H | 1998 Jul 1 | 9692922 |
| 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. | Liu JQ, Nagata S, Dairi T, Misono H, Shimizu S, Yamada H | 1997 Apr 15 | 9151955 |