EC number:4.2.3.155

Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.3 Acting on phosphates
ID:4.2.3.155
Description:2-epi-valiolone synthase.
Cath: 1.20.1090.10; 3.40.50.1970;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.3.155
BRENDA Enzyme Link: BRENDA 4.2.3.155
KEGG Enzyme Link: KEGG4.2.3.155
BioCyc Enzyme Link: BioCyc 4.2.3.155
ExPASy Enzyme Link: ExPASy4.2.3.155
EC2PDB Enzyme Link: EC2PDB 4.2.3.155
ExplorEnz Enzyme Link: ExplorEnz 4.2.3.155
PRIAM enzyme-specific profiles Link: PRIAM 4.2.3.155
IntEnz Enzyme Link: IntEnz 4.2.3.155
MEDLINE Enzyme Link: MEDLINE 4.2.3.155

EC number:4.2.3.155

MSA:

4.2.3.155;
Phylogenetic Tree:

4.2.3.155;
Uniprot:
M-CSA:
RHEA:49564 D-sedoheptulose 7-phosphate = 2-epi-valiolone + phosphate
RULE(radius=1) ([*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[O;H0;+0:6]-[CH2;+0:7]-[CH;+0:8](-[*:9])-[OH;+0:10])>>[*:1]-[C;H0;+0:2](-[*:3])(-[OH;+0:4])-[CH2;+0:7]-[C;H0;+0:8](-[*:9])=[O;H0;+0:10].[*:5]-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Evolutionary divergence of sedoheptulose 7-phosphate cyclases leads to several distinct cyclic products.Asamizu S, Xie P, Brumsted CJ, Flatt PM, Mahmud T2012 Jul 2522741921