Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.39
Description:Gluconate dehydratase.
Cath: 3.20.20.120; 3.30.390.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.39
BRENDA Enzyme Link: BRENDA 4.2.1.39
KEGG Enzyme Link: KEGG4.2.1.39
BioCyc Enzyme Link: BioCyc 4.2.1.39
ExPASy Enzyme Link: ExPASy4.2.1.39
EC2PDB Enzyme Link: EC2PDB 4.2.1.39
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.39
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.39
IntEnz Enzyme Link: IntEnz 4.2.1.39
MEDLINE Enzyme Link: MEDLINE 4.2.1.39
MSA:

4.2.1.39;

Phylogenetic Tree:

4.2.1.39;

Uniprot:
M-CSA:
RHEA:21612 D-gluconate = 2-dehydro-3-deoxy-D-gluconate + 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
The nonphosphorylative Entner-Doudoroff pathway in the thermoacidophilic euryarchaeon Picrophilus torridus involves a novel 2-keto-3-deoxygluconate- specific aldolase.Reher M, Fuhrer T, Bott M, Schönheit P2010 Feb20023024
The occurrence of a modified Entner-doudoroff pathway in Clostridium aceticum.Andreesen JR, Gottschalk G19695383859
Purification and properties of D-gluconate dehydratase from Clostridium pasteurianum.Bender R, Gottschalk G1973 Dec 34772682