Enzyme

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     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.2 Aldehyde-lyases
ID:4.1.2.29
Description:5-dehydro-2-deoxyphosphogluconate aldolase.
Alternative Name: Phospho-5-keto-2-deoxygluconate aldolase.
Phospho-5-dehydro-2-deoxygluconate aldolase.
5-dehydro-2-deoxy-D-gluconate-6-phosphate malonate-semialdehyde-lyase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.2.29
BRENDA Enzyme Link: BRENDA 4.1.2.29
KEGG Enzyme Link: KEGG4.1.2.29
BioCyc Enzyme Link: BioCyc 4.1.2.29
ExPASy Enzyme Link: ExPASy4.1.2.29
EC2PDB Enzyme Link: EC2PDB 4.1.2.29
ExplorEnz Enzyme Link: ExplorEnz 4.1.2.29
PRIAM enzyme-specific profiles Link: PRIAM 4.1.2.29
IntEnz Enzyme Link: IntEnz 4.1.2.29
MEDLINE Enzyme Link: MEDLINE 4.1.2.29
MSA:

4.1.2.29;

Phylogenetic Tree:

4.1.2.29;

Uniprot:
M-CSA:
RHEA:13177 6-phospho-5-dehydro-2-deoxy-D-gluconate = 3-oxopropanoate + dihydroxyacetone phosphate
RULE(radius=1) [*:1]-[CH;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[*:6]>>[*:5]-[CH2;+0:4]-[*:6].[*:1]-[CH;+0:2]=[O;H0;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The pathway of myo-inositol degradation in Aerobacter aerogenes. Conversion of 2-deoxy-5-keto-D-gluconic acid to glycolytic intermediates.Anderson WA, Magasanik B1971 Sep 254328832
myo-Inositol catabolism in Bacillus subtilis.Yoshida K, Yamaguchi M, Morinaga T, Kinehara M, Ikeuchi M, Ashida H, Fujita Y2008 Apr 1818310071