EC number:2.8.2.32

Enzyme

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     2. Transferases
        2.8 Transferring sulfur-containing groups
            2.8.2 Sulfotransferases
ID:2.8.2.32
Description:Scymnol sulfotransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.8.2.32
BRENDA Enzyme Link: BRENDA 2.8.2.32
KEGG Enzyme Link: KEGG2.8.2.32
BioCyc Enzyme Link: BioCyc 2.8.2.32
ExPASy Enzyme Link: ExPASy2.8.2.32
EC2PDB Enzyme Link: EC2PDB 2.8.2.32
ExplorEnz Enzyme Link: ExplorEnz 2.8.2.32
PRIAM enzyme-specific profiles Link: PRIAM 2.8.2.32
IntEnz Enzyme Link: IntEnz 2.8.2.32
MEDLINE Enzyme Link: MEDLINE 2.8.2.32

EC number:2.8.2.32

MSA:

2.8.2.32;
Phylogenetic Tree:

2.8.2.32;
Uniprot:
M-CSA:
RHEA:15477 3'-phosphoadenylyl sulfate + 5beta-scymnol = 5beta-scymnol sulfate + adenosine 3',5'-bisphosphate + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[S;H0;+0:3](=[*:4])(=[*:5])-[*:6].[*:7]-[OH;+0:8]>>[*:1]-[OH;+0:2].[*:4]=[S;H0;+0:3](=[*:5])(-[*:6])-[O;H0;+0:8]-[*:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Enzymic sulfation of bile salts. Partial purification and characterization of an enzyme from the liver of the shark Heterodontus portusjacksoni that catalyses the sulfation of the shark bile steroid 5 beta-scymnol.Macrides TA, Faktor DA, Kalafatis N, Amiet RG1994 Mar7749614