EC number:4.1.1.12
| ID: | 4.1.1.12 |
|---|---|
| Description: | Aspartate 4-decarboxylase. |
| Alternative Name: |
L-aspartate 4-carboxy-lyase. Desulfinase. |
| Cath: | 1.10.20.110; 3.90.1150.10; |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.1.12 |
| BRENDA Enzyme Link: | BRENDA 4.1.1.12 |
| KEGG Enzyme Link: | KEGG4.1.1.12 |
| BioCyc Enzyme Link: | BioCyc 4.1.1.12 |
| ExPASy Enzyme Link: | ExPASy4.1.1.12 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.1.12 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.1.12 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.1.12 |
| IntEnz Enzyme Link: | IntEnz 4.1.1.12 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.1.12 |
| RHEA:12621 | H(+) + L-aspartate = CO2 + L-alanine |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[OH;+0:3])-[CH2;+0:4]-[*:5].[H+;H0:6]>>[*:5]-[CH3;+0:4].[*: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 |
|---|---|---|---|
| Some stereochemical features of aspartate beta-decarboxylase. | Chang CC, Laghai A, O'Leary MH, Floss HG | 1982 Apr 10 | 7037785 |
| Aspartate beta-decarboxylase from Alcaligenes faecalis: carbon-13 kinetic isotope effect and deuterium exchange experiments. | Rosenberg RM, O'Leary MH | 1985 Mar 26 | 4005219 |
| Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase. | Chen HJ, Ko TP, Lee CY, Wang NC, Wang AH | 2009 Apr 15 | 19368885 |
| Molecular cloning of the aspartate 4-decarboxylase gene from Pseudomonas sp. ATCC 19121 and characterization of the bifunctional recombinant enzyme. | Wang NC, Lee CY | 2006 Nov | 16847601 |