Enzyme

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EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.2 Aldehyde-lyases
ID:4.1.2.57
Description:Sulfofructosephosphate aldolase.
Cath: 3.20.20.70;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.2.57
BRENDA Enzyme Link: BRENDA 4.1.2.57
KEGG Enzyme Link: KEGG4.1.2.57
BioCyc Enzyme Link: BioCyc 4.1.2.57
ExPASy Enzyme Link: ExPASy4.1.2.57
EC2PDB Enzyme Link: EC2PDB 4.1.2.57
ExplorEnz Enzyme Link: ExplorEnz 4.1.2.57
PRIAM enzyme-specific profiles Link: PRIAM 4.1.2.57
IntEnz Enzyme Link: IntEnz 4.1.2.57
MEDLINE Enzyme Link: MEDLINE 4.1.2.57
MSA:

4.1.2.57;

Phylogenetic Tree:

4.1.2.57;

Uniprot:
M-CSA:
RHEA:40515 6-deoxy-6-sulfo-D-fructose 1-phosphate = 3-sulfolactaldehyde + dihydroxyacetone phosphate
RULE(radius=1) [*:1]-[CH;+0:2]1-[CH;+0:3](-[OH;+0:4])-[*:5]-[O;H0;+0:6]-[C;H0;+0:7]-1(-[*:8])-[OH;+0:9]>>[*:1]-[CH2;+0:2]-[C;H0;+0:7](-[*:8])=[O;H0;+0:9].[O;H0;+0:4]=[CH;+0:3]-[*:5]-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle.Denger K, Weiss M, Felux AK, Schneider A, Mayer C, Spiteller D, Huhn T, Cook AM, Schleheck D2014 Mar 624463506