EC number:4.1.3.14
| ID: | 4.1.3.14 |
|---|---|
| Description: | L-erythro-3-hydroxyaspartate aldolase. |
| Alternative Name: |
Erythro-3-hydroxy-L(s)-aspartate glyoxylate-lyase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.3.14 |
| BRENDA Enzyme Link: | BRENDA 4.1.3.14 |
| KEGG Enzyme Link: | KEGG4.1.3.14 |
| BioCyc Enzyme Link: | BioCyc 4.1.3.14 |
| ExPASy Enzyme Link: | ExPASy4.1.3.14 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.3.14 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.3.14 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.3.14 |
| IntEnz Enzyme Link: | IntEnz 4.1.3.14 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.3.14 |
| RHEA:14377 | (3R)-3-hydroxy-L-aspartate = glycine + glyoxylate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[*:6]>>[*:5]-[CH2;+0:4]-[*:6].[*:1]-[CH;+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 |
|---|---|---|---|
| ASSAY AND PROPERTIES OF BETA-HYDROXYASPARTATE ALDOLASE FROM MICROCOCCUS DENITRIFICANS. | GIBBS RG, MORRIS JG | 1964 Jun 1 | 14194868 |