EC number:4.2.1.158

Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.158
Description:Galactarate dehydratase (D-threo-forming).
Cath: 3.20.20.120; 3.30.390.10; 3.90.1210.30;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.158
BRENDA Enzyme Link: BRENDA 4.2.1.158
KEGG Enzyme Link: KEGG4.2.1.158
BioCyc Enzyme Link: BioCyc 4.2.1.158
ExPASy Enzyme Link: ExPASy4.2.1.158
EC2PDB Enzyme Link: EC2PDB 4.2.1.158
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.158
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.158
IntEnz Enzyme Link: IntEnz 4.2.1.158
MEDLINE Enzyme Link: MEDLINE 4.2.1.158

EC number:4.2.1.158

MSA:

4.2.1.158;
Phylogenetic Tree:

4.2.1.158;
Uniprot:
M-CSA:
RHEA:45808 galactarate = (2S,3R)-dihydroxy-5-oxohexanedioate + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[CH2;+0:4]-[*:5].[OH2;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Computation-facilitated assignment of the function in the enolase superfamily: a regiochemically distinct galactarate dehydratase from Oceanobacillus iheyensis .Rakus JF, Kalyanaraman C, Fedorov AA, Fedorov EV, Mills-Groninger FP, Toro R, Bonanno J, Bain K, Sauder JM, Burley SK, Almo SC, Jacobson MP, Gerlt JA2009 Dec 819883118