Enzyme

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EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.3 Oxo-acid-lyases
ID:4.1.3.42
Description:(4S)-4-hydroxy-2-oxoglutarate aldolase.
Alternative Name: Hydroxyketoglutaric aldolase.
4-hydroxy-2-ketoglutaric aldolase.
2-keto-4-hydroxyglutaric aldolase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.3.42
BRENDA Enzyme Link: BRENDA 4.1.3.42
KEGG Enzyme Link: KEGG4.1.3.42
BioCyc Enzyme Link: BioCyc 4.1.3.42
ExPASy Enzyme Link: ExPASy4.1.3.42
EC2PDB Enzyme Link: EC2PDB 4.1.3.42
ExplorEnz Enzyme Link: ExplorEnz 4.1.3.42
PRIAM enzyme-specific profiles Link: PRIAM 4.1.3.42
IntEnz Enzyme Link: IntEnz 4.1.3.42
MEDLINE Enzyme Link: MEDLINE 4.1.3.42
MSA:

4.1.3.42;

Phylogenetic Tree:

4.1.3.42;

Uniprot:
M-CSA:
RHEA:35639 L-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[CH2;+0:4]-[CH;+0:5](-[*:6])-[OH;+0:7]>>[*:6]-[C;H0;+0:5](-[CH3;+0:4])=[O;H0;+0:7].[*:1]-[CH;+0:2]=[*:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification, substrate specificity and binding, -decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase.Nishihara H, Dekker EE1972 Aug 254560498
Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene.Patil RV, Dekker EE1992 Jan1339418