EC number:2.8.2.38

Enzyme

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     2. Transferases
        2.8 Transferring sulfur-containing groups
            2.8.2 Sulfotransferases
ID:2.8.2.38
Description:Aliphatic desulfoglucosinolate sulfotransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.8.2.38
BRENDA Enzyme Link: BRENDA 2.8.2.38
KEGG Enzyme Link: KEGG2.8.2.38
BioCyc Enzyme Link: BioCyc 2.8.2.38
ExPASy Enzyme Link: ExPASy2.8.2.38
EC2PDB Enzyme Link: EC2PDB 2.8.2.38
ExplorEnz Enzyme Link: ExplorEnz 2.8.2.38
PRIAM enzyme-specific profiles Link: PRIAM 2.8.2.38
IntEnz Enzyme Link: IntEnz 2.8.2.38
MEDLINE Enzyme Link: MEDLINE 2.8.2.38

EC number:2.8.2.38

MSA:

2.8.2.38;
Phylogenetic Tree:

2.8.2.38;
Uniprot:
M-CSA:
RHEA:52724 3'-phosphoadenylyl sulfate + an aliphatic desulfo-glucosinolate = adenosine 3',5'-bisphosphate + an omega-(methylsulfanyl)-N-sulfo-alkylhydroximate S-glucoside + 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
Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana catalyze the final step in the biosynthesis of the glucosinolate core structure.Piotrowski M, Schemenewitz A, Lopukhina A, Müller A, Janowitz T, Weiler EW, Oecking C2004 Dec 315358770
Kinetics and substrate specificities of desulfo-glucosinolate sulfotransferases in Arabidopsis thaliana.Klein M, Papenbrock J2009 Feb19077143
The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis have different substrate specificities and are differentially expressed.Klein M, Reichelt M, Gershenzon J, Papenbrock J2006 Jan16367753