Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.3 Acting on phosphates
ID:4.2.3.152
Description:2-epi-5-epi-valiolone synthase.
Alternative Name: C(7)-cyclitol synthase.
Cath: 1.20.1090.10; 3.40.50.1970;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.3.152
BRENDA Enzyme Link: BRENDA 4.2.3.152
KEGG Enzyme Link: KEGG4.2.3.152
BioCyc Enzyme Link: BioCyc 4.2.3.152
ExPASy Enzyme Link: ExPASy4.2.3.152
EC2PDB Enzyme Link: EC2PDB 4.2.3.152
ExplorEnz Enzyme Link: ExplorEnz 4.2.3.152
PRIAM enzyme-specific profiles Link: PRIAM 4.2.3.152
IntEnz Enzyme Link: IntEnz 4.2.3.152
MEDLINE Enzyme Link: MEDLINE 4.2.3.152
MSA:

4.2.3.152;

Phylogenetic Tree:

4.2.3.152;

Uniprot:
M-CSA:
RHEA:44184 D-sedoheptulose 7-phosphate = 2-epi-5-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
2-epi-5-epi-Valiolone synthase activity is essential for maintaining phycobilisome composition in the cyanobacterium Anabaena variabilis ATCC 29413 when grown in the presence of a carbon source.Spence E, Bryan SJ, Lisfi M, Cullum J, Dunlap WC, Shick JM, Mullineaux CW, Long PF2013 Sep23857509
ValC, a new type of C7-Cyclitol kinase involved in the biosynthesis of the antifungal agent validamycin A.Minagawa K, Zhang Y, Ito T, Bai L, Deng Z, Mahmud T2007 Apr 1617335096
Synthesis of 5-epi-[6-(2)H(2)]valiolone and stereospecifically monodeuterated 5-epi-valiolones: exploring the steric course of 5-epi-valiolone dehydratase in validamycin A biosynthesis.Mahmud T, Xu J, Choi YU2001 Jul 2711463258