EC number:4.2.1.141

Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.141
Description:2-dehydro-3-deoxy-D-arabinonate dehydratase.
Cath: 3.90.850.10; 3.10.330.40;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.141
BRENDA Enzyme Link: BRENDA 4.2.1.141
KEGG Enzyme Link: KEGG4.2.1.141
BioCyc Enzyme Link: BioCyc 4.2.1.141
ExPASy Enzyme Link: ExPASy4.2.1.141
EC2PDB Enzyme Link: EC2PDB 4.2.1.141
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.141
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.141
IntEnz Enzyme Link: IntEnz 4.2.1.141
MEDLINE Enzyme Link: MEDLINE 4.2.1.141

EC number:4.2.1.141

MSA:

4.2.1.141;
Phylogenetic Tree:

4.2.1.141;
Uniprot:
M-CSA:
RHEA:35807 2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[OH;+0:3])-[CH2;+0:4]-[OH;+0:5]>>[*:1]-[CH2;+0:2]-[CH;+0:4]=[O;H0;+0:5].[OH2;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural insight into substrate binding and catalysis of a novel 2-keto-3-deoxy-D-arabinonate dehydratase illustrates common mechanistic features of the FAH superfamily.Brouns SJ, Barends TR, Worm P, Akerboom J, Turnbull AP, Salmon L, van der Oost J2008 May 3018448118
Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment.Brouns SJ, Walther J, Snijders AP, van de Werken HJ, Willemen HL, Worm P, de Vos MG, Andersson A, Lundgren M, Mazon HF, van den Heuvel RH, Nilsson P, Salmon L, de Vos WM, Wright PC, Bernander R, van der Oost J2006 Sep 1516849334