Enzyme

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     4. Lyases
        4.3 Carbon-nitrogen lyases
            4.3.1 Ammonia-lyases
ID:4.3.1.16
Description:Threo-3-hydroxy-L-aspartate ammonia-lyase.
Alternative Name: Threo-3-hydroxyaspartate dehydratase.
L-threo-3-hydroxyaspartate dehydratase.
Cath: 3.20.20.10; 2.40.37.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.3.1.16
BRENDA Enzyme Link: BRENDA 4.3.1.16
KEGG Enzyme Link: KEGG4.3.1.16
BioCyc Enzyme Link: BioCyc 4.3.1.16
ExPASy Enzyme Link: ExPASy4.3.1.16
EC2PDB Enzyme Link: EC2PDB 4.3.1.16
ExplorEnz Enzyme Link: ExplorEnz 4.3.1.16
PRIAM enzyme-specific profiles Link: PRIAM 4.3.1.16
IntEnz Enzyme Link: IntEnz 4.3.1.16
MEDLINE Enzyme Link: MEDLINE 4.3.1.16
MSA:

4.3.1.16;

Phylogenetic Tree:

4.3.1.16;

Uniprot:
M-CSA:
RHEA:12424 (3S)-3-hydroxy-L-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

References

TitleAuthorsDatePubMed ID
Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3-hydroxyaspartate dehydratase activity.Wada M, Nakamori S, Takagi H2003 Aug 2912951240
Purification and characterization of a novel enzyme, L-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62.Wada M, Matsumoto T, Nakamori S, Sakamoto M, Kataoka M, Liu JQ, Itoh N, Yamada H, Shimizu S1999 Oct 110481099