EC number:2.8.2.37

Enzyme

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EC Tree
     2. Transferases
        2.8 Transferring sulfur-containing groups
            2.8.2 Sulfotransferases
ID:2.8.2.37
Description:Trehalose 2-sulfotransferase.
Cath: 3.40.50.300;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.8.2.37
BRENDA Enzyme Link: BRENDA 2.8.2.37
KEGG Enzyme Link: KEGG2.8.2.37
BioCyc Enzyme Link: BioCyc 2.8.2.37
ExPASy Enzyme Link: ExPASy2.8.2.37
EC2PDB Enzyme Link: EC2PDB 2.8.2.37
ExplorEnz Enzyme Link: ExplorEnz 2.8.2.37
PRIAM enzyme-specific profiles Link: PRIAM 2.8.2.37
IntEnz Enzyme Link: IntEnz 2.8.2.37
MEDLINE Enzyme Link: MEDLINE 2.8.2.37

EC number:2.8.2.37

MSA:

2.8.2.37;
Phylogenetic Tree:

2.8.2.37;
Uniprot:
M-CSA:
RHEA:41608 3'-phosphoadenylyl sulfate + alpha,alpha-trehalose = 2-O-sulfo-alpha,alpha-trehalose + 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
Kinetic measurements and mechanism determination of Stf0 sulfotransferase using mass spectrometry.Pi N, Hoang MB, Gao H, Mougous JD, Bertozzi CR, Leary JA2005 Jun 115866533
Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis.Mougous JD, Petzold CJ, Senaratne RH, Lee DH, Akey DL, Lin FL, Munchel SE, Pratt MR, Riley LW, Leary JA, Berger JM, Bertozzi CR2004 Aug15258569