| ID: | 4.1.1.73 |
|---|---|
| Description: | Tartrate decarboxylase. |
| Alternative Name: |
(R,R)-tartrate carboxy-lyase. |
| Cath: | 3.40.718.10; |
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 4.1.1.73 |
| BRENDA Enzyme Link: | BRENDA 4.1.1.73 |
| KEGG Enzyme Link: | KEGG4.1.1.73 |
| BioCyc Enzyme Link: | BioCyc 4.1.1.73 |
| ExPASy Enzyme Link: | ExPASy4.1.1.73 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.1.73 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.1.73 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.1.73 |
| IntEnz Enzyme Link: | IntEnz 4.1.1.73 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.1.73 |
| RHEA:13317 | (2R,3R)-tartrate + H(+) = CO2 + D-glycerate |
| 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and characterization of a new NAD(+)-dependent enzyme, L-tartrate decarboxylase, from Pseudomonas sp. group Ve-2. | Furuyoshi S, Nawa Y, Kawabata N, Tanaka H, Soda K | 1991 Oct | 1778975 |