Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.8.2.38 extracted from

  • Hirschmann, F.; Krause, F.; Baruch, P.; Chizhov, I.; Mueller, J.W.; Manstein, D.J.; Papenbrock, J.; Fedorov, R.
    Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism (2017), Sci. Rep., 7, 4160 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant AtSOT18 in complex with PAP alone and together with the glycosinolate sinigrin, X-ray diffraction structure determination and analysis at 1.74-1.92 A resolution Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
H155A site-directed mutagenesis, inactive mutant Arabidopsis thaliana
K93A site-directed mutagenesis, inactive mutant Arabidopsis thaliana
P136A site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type enzyme Arabidopsis thaliana
T96A site-directed mutagenesis, mutant Thr96Ala shows residual activity with the preferred substrates 3-methylthiopropyl desulfoglucosinolate and 8-methylthiooctyl desulfoglucosinolate (12fold reduction and 3fold reduction, respectively), while with sinigrin no activity is detected Arabidopsis thaliana
T97A site-directed mutagenesis, inactive mutant Arabidopsis thaliana
Y130A site-directed mutagenesis, inactive mutant Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
adenosine 3',5'-bisphosphate PAP, competitive inhibition Arabidopsis thaliana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Arabidopsis thaliana 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3'-phosphoadenylyl sulfate + desulfosinigrin Arabidopsis thaliana
-
adenosine 3',5'-bisphosphate + sinigrin
-
?
3'-phosphoadenylyl sulfate + desulfosinigrin Arabidopsis thaliana Col-0
-
adenosine 3',5'-bisphosphate + sinigrin
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9C9C9
-
-
Arabidopsis thaliana Col-0 Q9C9C9
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0073
-
recombinant mutant T96A, substrate 3-methylthiopropyl desulfoglucosinolate, pH 8.0, 37°C Arabidopsis thaliana
0.028
-
recombinant mutant P136A, substrate glucobrassicin, pH 8.0, 37°C Arabidopsis thaliana
0.03
-
recombinant wild-type enzyme, substrate glucobrassicin, pH 8.0, 37°C Arabidopsis thaliana
0.032
-
recombinant mutant T96A, substrate 8-methylthiooctyl desulfoglucosinolate, pH 8.0, 37°C Arabidopsis thaliana
0.053
-
recombinant wild-type enzyme, substrate sinigrin, pH 8.0, 37°C Arabidopsis thaliana
0.0971
-
recombinant wild-type enzyme, substrate 8-methylthiooctyl desulfoglucosinolate, pH 8.0, 37°C Arabidopsis thaliana
0.0974
-
recombinant wild-type enzyme, substrate 3-methylthiopropyl desulfoglucosinolate, pH 8.0, 37°C Arabidopsis thaliana
0.104
-
recombinant mutant P136A, substrate 3-methylthiopropyl desulfoglucosinolate, pH 8.0, 37°C Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3'-phosphoadenylyl sulfate + 3-methylthiopropyl desulfoglucosinolate
-
Arabidopsis thaliana adenosine 3',5'-bisphosphate + 3-methylthiopropyl glucosinolate
-
?
3'-phosphoadenylyl sulfate + 3-methylthiopropyl desulfoglucosinolate
-
Arabidopsis thaliana Col-0 adenosine 3',5'-bisphosphate + 3-methylthiopropyl glucosinolate
-
?
3'-phosphoadenylyl sulfate + desulfosinigrin
-
Arabidopsis thaliana adenosine 3',5'-bisphosphate + sinigrin
-
?
3'-phosphoadenylyl sulfate + desulfosinigrin
-
Arabidopsis thaliana Col-0 adenosine 3',5'-bisphosphate + sinigrin
-
?
adenosine 3',5'-bisphosphate + 7-methylthioheptyl glucosinolate
-
Arabidopsis thaliana 3'-phosphoadenylyl sulfate + 7-methylthioheptyl desulfoglucosinolate
-
?
adenosine 3',5'-bisphosphate + 7-methylthioheptyl glucosinolate
-
Arabidopsis thaliana Col-0 3'-phosphoadenylyl sulfate + 7-methylthioheptyl desulfoglucosinolate
-
?
adenosine 3',5'-bisphosphate + 8-methylthiooctyl glucosinolate
-
Arabidopsis thaliana 3'-phosphoadenylyl sulfate + 8-methylthiooctyl desulfoglucosinolate
-
?
adenosine 3',5'-bisphosphate + 8-methylthiooctyl glucosinolate
-
Arabidopsis thaliana Col-0 3'-phosphoadenylyl sulfate + 8-methylthiooctyl desulfoglucosinolate
-
?
adenosine 3',5'-bisphosphate + sinigrin sinigrin binding is facilitated by hydrogen bonding with residues Arg51, Glu54, Thr96, Tyr130, His155 and Tyr306. The guanidinium group of Arg51 interacts with the 6'-hydroxyl group of the glucopyranose of the glucosinolate. The carboxyl group of Glu54 interacts with the 4'- and the 6'-hydroxyl groups. The hydroxyl of Tyr306 forms a hydrogen bond with the oxygen in the glucopyranose ring. The sulfate moiety is stabilized by hydrogen bonds with Thr96, Tyr130 and His155. In this positioning the sulfate and phosphate groups of sinigrin and PAP, respectively, are located within the hydrogen bond distance from each other. Analysis of the mechanism of PAPS binding Arabidopsis thaliana 3'-phosphoadenylyl sulfate + desulfosinigrin
-
?
additional information enzyme AtSOT18 prefers the long-chain ds-Gls 7-methylthioheptyl Gl and 8-methylthiooctyl Gl (8MTO), that are also derived from methionine Arabidopsis thaliana ?
-
-
additional information enzyme AtSOT18 prefers the long-chain ds-Gls 7-methylthioheptyl Gl and 8-methylthiooctyl Gl (8MTO), that are also derived from methionine Arabidopsis thaliana Col-0 ?
-
-

Subunits

Subunits Comment Organism
More AtSOT18 does not contain the dimerization motif KxxxTVxxxE Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
3'-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfotransferase UniProt Arabidopsis thaliana
AtSOT18
-
Arabidopsis thaliana
cytosolic sulfotransferase 18
-
Arabidopsis thaliana
desulpho-Gl SOT
-
Arabidopsis thaliana
ds-Gl SOT
-
Arabidopsis thaliana
SOT18
-
Arabidopsis thaliana
sulphotransferase 18
-
Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Arabidopsis thaliana

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
95
-
purified enzyme, 10 min, pH 8.0, inactivation Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Arabidopsis thaliana

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics Arabidopsis thaliana

General Information

General Information Comment Organism
evolution sulfotransferases (SOTs or SULTs) can be found in all organisms analysed so far. In Arabidopsis thaliana, twenty-two sulfotransferase (SOT) isoforms are identified. Three of those are involved in glucosinolate (Gl) biosynthesis, glycosylated sulfur-containing aldoximes containing chemically different side chains, whose breakdown products are involved in stress response against herbivores, pathogens, and abiotic stress. The structure of AtSOT18 invigorates the similarity between plant and mammalian sulfotransferases, which illustrates the evolutionary conservation of this multifunctional enzyme family. In Arabidopsis thaliana, the three SOTs AtSOT16, AtSOT17 and AtSOT18 exclusively catalyse the transfer of a sulfuryl group to different ds-Gls. All three enzymes are localized in the cytoplasm and their expression pattern tested under several conditions is similar. They show 72% sequence identity but differ remarkably in their substrate specificity Arabidopsis thaliana
additional information structure homology modeling Arabidopsis thaliana
physiological function sulfotransferases catalyse the transfer of a sulfuryl group from the co-substrate 3'-phospho-adenosine 5'-phosphosulfate (PAPS) to a hydroxyl group of various substrates. In plants, sulfated compounds act as hormones, secondary metabolites in stress defense and probably serve as a reservoir for sulfur Arabidopsis thaliana