EC number:4.1.1.11
| ID: | 4.1.1.11 |
|---|---|
| Description: | Aspartate 1-decarboxylase. |
| Alternative Name: |
L-aspartate 1-carboxy-lyase. Aspartate alpha-decarboxylase. |
| Cath: | 3.40.1260.20; 3.40.640.10; 3.90.1150.10; 2.40.40.20; 2.40.50.140; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.1.11 |
| BRENDA Enzyme Link: | BRENDA 4.1.1.11 |
| KEGG Enzyme Link: | KEGG4.1.1.11 |
| BioCyc Enzyme Link: | BioCyc 4.1.1.11 |
| ExPASy Enzyme Link: | ExPASy4.1.1.11 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.1.11 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.1.11 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.1.11 |
| IntEnz Enzyme Link: | IntEnz 4.1.1.11 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.1.11 |
| RHEA:19497 | H(+) + L-aspartate = beta-alanine + CO2 |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[C;H0;+0:4](=[*:5])-[OH;+0:6].[H+;H0:7]>>[*:1]-[CH2;+0:2]-[*:3].[*:5]=[C;H0;+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 |
|---|---|---|---|
| Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. | Albert A, Dhanaraj V, Genschel U, Khan G, Ramjee MK, Pulido R, Sibanda BL, von Delft F, Witty M, Blundell TL, Smith AG, Abell C | 1998 Apr | 9546220 |
| Crystal structure of uncleaved L-aspartate-alpha-decarboxylase from Mycobacterium tuberculosis. | Gopalan G, Chopra S, Ranganathan A, Swaminathan K | 2006 Dec 1 | 17001646 |
| Crystal structure of the schiff base intermediate prior to decarboxylation in the catalytic cycle of aspartate alpha-decarboxylase. | Lee BI, Suh SW | 2004 Jun 25 | 15184017 |