| ID: | 4.3.1.19 | ||
|---|---|---|---|
| Description: | Threonine ammonia-lyase. | ||
| Alternative Name: |
Threonine dehydratase. Threonine dehydrase. Threonine deaminase. Serine deaminase. L-threonine hydro-lyase (deaminating). L-threonine dehydratase. L-threonine deaminase. L-serine dehydratase. | ||
| Prosite: | PDOC00149; | ||
| PDB: |
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| Cath: | 3.30.1330.40; 3.30.1330.90; 3.40.1020.10; 3.40.50.1100; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 4.3.1.19 |
| BRENDA Enzyme Link: | BRENDA 4.3.1.19 |
| KEGG Enzyme Link: | KEGG4.3.1.19 |
| BioCyc Enzyme Link: | BioCyc 4.3.1.19 |
| ExPASy Enzyme Link: | ExPASy4.3.1.19 |
| EC2PDB Enzyme Link: | EC2PDB 4.3.1.19 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.3.1.19 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.3.1.19 |
| IntEnz Enzyme Link: | IntEnz 4.3.1.19 |
| MEDLINE Enzyme Link: | MEDLINE 4.3.1.19 |
| RHEA:22108 | L-threonine = 2-oxobutanoate + NH4(+) |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:6])-[CH2;+0:4]-[*:5].[NH3;+0:3] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Regulation of isoleucine-valine biosynthesis in Saccharomyces cerevisiae. | Holmberg S, Petersen JG | 1988 Mar | 3289762 |
| A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies. | Yamada T, Komoto J, Kasuya T, Takata Y, Ogawa H, Mori H, Takusagawa F | 2008 May | 18342636 |
| Elucidation of an alternate isoleucine biosynthesis pathway in Geobacter sulfurreducens. | Risso C, Van Dien SJ, Orloff A, Lovley DR, Coppi MV | 2008 Apr | 18245290 |
| Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation. | Simanshu DK, Savithri HS, Murthy MR | 2006 Dec 22 | 17046821 |
| Serine and threonine desaminaes of Escherichia coli; activators for a cell-free enzyme. | WOOD WA, GUNSALUS IC | 1949 Nov | 15390404 |