Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.42
Description:Galactarate dehydratase.
Alternative Name: D-galactarate hydro-lyase.
Cath: 3.20.20.120; 3.30.390.10; 3.90.1210.30;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.42
BRENDA Enzyme Link: BRENDA 4.2.1.42
KEGG Enzyme Link: KEGG4.2.1.42
BioCyc Enzyme Link: BioCyc 4.2.1.42
ExPASy Enzyme Link: ExPASy4.2.1.42
EC2PDB Enzyme Link: EC2PDB 4.2.1.42
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.42
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.42
IntEnz Enzyme Link: IntEnz 4.2.1.42
MEDLINE Enzyme Link: MEDLINE 4.2.1.42
MSA:

4.2.1.42;

Phylogenetic Tree:

4.2.1.42;

Uniprot:
M-CSA:
RHEA:16005 galactarate = 5-dehydro-4-deoxy-D-glucarate + 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
Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli.Hubbard BK, Koch M, Palmer DR, Babbitt PC, Gerlt JA1998 Oct 139772162
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
Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2.Yew WS, Fedorov AA, Fedorov EV, Almo SC, Gerlt JA2007 Aug 2117649980