EC number:4.1.1.81
| ID: | 4.1.1.81 |
|---|---|
| Description: | Threonine-phosphate decarboxylase. |
| Alternative Name: |
L-threonine-O-3-phosphate decarboxylase. L-threonine O-3-phosphate carboxy-lyase. |
| Cath: | 3.40.640.10; 3.90.1150.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.1.81 |
| BRENDA Enzyme Link: | BRENDA 4.1.1.81 |
| KEGG Enzyme Link: | KEGG4.1.1.81 |
| BioCyc Enzyme Link: | BioCyc 4.1.1.81 |
| ExPASy Enzyme Link: | ExPASy4.1.1.81 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.1.81 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.1.81 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.1.81 |
| IntEnz Enzyme Link: | IntEnz 4.1.1.81 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.1.81 |
| RHEA:11492 | H(+) + O-phospho-L-threonine = (R)-1-aminopropan-2-yl phosphate + CO2 |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[*:6].[H+;H0:7]>>[*:5]-[CH2;+0:4]-[*:6].[*:1]=[C;H0;+0:2]=[O;H0;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2. | Brushaber KR, O'Toole GA, Escalante-Semerena JC | 1998 Jan 30 | 9446573 |
| The biosynthesis of adenosylcobalamin (vitamin B12). | Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC | 2002 Aug | 12195810 |
| Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica. | Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I | 2002 Apr 16 | 11939774 |