ID: | 4.3.1.27 |
---|---|
Description: | Threo-3-hydroxy-D-aspartate ammonia-lyase. |
Alternative Name: |
D-threo-3-hydroxyaspartate dehydratase. |
Cath: | 3.20.20.10; 2.40.37.20; |
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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 4.3.1.27 |
BRENDA Enzyme Link: | BRENDA 4.3.1.27 |
KEGG Enzyme Link: | KEGG4.3.1.27 |
BioCyc Enzyme Link: | BioCyc 4.3.1.27 |
ExPASy Enzyme Link: | ExPASy4.3.1.27 |
EC2PDB Enzyme Link: | EC2PDB 4.3.1.27 |
ExplorEnz Enzyme Link: | ExplorEnz 4.3.1.27 |
PRIAM enzyme-specific profiles Link: | PRIAM 4.3.1.27 |
IntEnz Enzyme Link: | IntEnz 4.3.1.27 |
MEDLINE Enzyme Link: | MEDLINE 4.3.1.27 |
RHEA:27942 | (3R)-3-hydroxy-D-aspartate = NH4(+) + oxaloacetate |
RULE(radius=1) | [*:1]-[CH;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[NH2;+0:6]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[CH2;+0:4]-[*:5].[NH3;+0:6] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Purification, characterization and amino acid sequence of a novel enzyme, D-threo-3-hydroxyaspartate dehydratase, from Delftia sp. HT23. | Maeda T, Takeda Y, Murakami T, Yokota A, Wada M | 2010 Dec | 20843822 |