Enzyme

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EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.2 Aldehyde-lyases
ID:4.1.2.21
Description:2-dehydro-3-deoxy-6-phosphogalactonate aldolase.
Alternative Name: 6-phospho-2-keto-3-deoxygalactonate aldolase.
6-phospho-2-dehydro-3-deoxygalactonate aldolase.
2-oxo-3-deoxygalactonate 6-phosphate aldolase.
2-dehydro-3-deoxyphosphogalactonate aldolase.
lyase.
2-dehydro-3-deoxy-D-galactonate-6-phosphate D-glyceraldehyde-3-phosphate-
Cath: 3.20.20.70;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.2.21
BRENDA Enzyme Link: BRENDA 4.1.2.21
KEGG Enzyme Link: KEGG4.1.2.21
BioCyc Enzyme Link: BioCyc 4.1.2.21
ExPASy Enzyme Link: ExPASy4.1.2.21
EC2PDB Enzyme Link: EC2PDB 4.1.2.21
ExplorEnz Enzyme Link: ExplorEnz 4.1.2.21
PRIAM enzyme-specific profiles Link: PRIAM 4.1.2.21
IntEnz Enzyme Link: IntEnz 4.1.2.21
MEDLINE Enzyme Link: MEDLINE 4.1.2.21
MSA:

4.1.2.21;

Phylogenetic Tree:

4.1.2.21;

Uniprot:
M-CSA:
RHEA:24464 2-dehydro-3-deoxy-6-phospho-D-galactonate = D-glyceraldehyde 3-phosphate + pyruvate
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH;+0:3](-[*:4])-[OH;+0:5]>>[*:1]-[CH3;+0:2].[*:4]-[CH;+0:3]=[O;H0;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Characterization and crystal structure of Escherichia coli KDPGal aldolase.Walters MJ, Srikannathasan V, McEwan AR, Naismith JH, Fierke CA, Toone EJ2008 Jan 1517981470