EC number:4.2.1.43

Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.43
Description:2-dehydro-3-deoxy-L-arabinonate dehydratase.
Alternative Name: 2-keto-3-deoxy-L-arabinonate dehydratase.
Cath: 3.20.20.70;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.43
BRENDA Enzyme Link: BRENDA 4.2.1.43
KEGG Enzyme Link: KEGG4.2.1.43
BioCyc Enzyme Link: BioCyc 4.2.1.43
ExPASy Enzyme Link: ExPASy4.2.1.43
EC2PDB Enzyme Link: EC2PDB 4.2.1.43
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.43
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.43
IntEnz Enzyme Link: IntEnz 4.2.1.43
MEDLINE Enzyme Link: MEDLINE 4.2.1.43

EC number:4.2.1.43

MSA:

4.2.1.43;
Phylogenetic Tree:

4.2.1.43;
Uniprot:
M-CSA:
RHEA:17201 2-dehydro-3-deoxy-L-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
Studies on the mechanism of action of 2-keto-3-deoxy-L-arabonate dehydratase. The participation of an enzyme-substrate Schiff base in a dehydration.Portsmouth D, Stoolmiller AC, Abeles RH1967 Jun 106027246
Formation of alpha-ketoglutaric semialdehyde from L-2-keto-3-deoxyarabonic acid and isolation of L-2-keto-3-deoxyarabonate dehydratase from Pseudomonas saccharophila.Stoolmiller AC, Abeles RH1966 Dec 255954356
Preliminary crystallographic analysis of L-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of L-arabinose metabolism.Shimada N, Mikami B, Watanabe S, Makino K2007 May 117565178
Identification and characterization of L-arabonate dehydratase, L-2-keto-3-deoxyarabonate dehydratase, and L-arabinolactonase involved in an alternative pathway of L-arabinose metabolism. Novel evolutionary insight into sugar metabolism.Watanabe S, Shimada N, Tajima K, Kodaki T, Makino K2006 Nov 316950779