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Information on EC 2.8.2.38 - aliphatic desulfoglucosinolate sulfotransferase
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EC Tree
2.8.2.38 aliphatic desulfoglucosinolate sulfotransferaseIUBMB Comments
The enzyme catalyses the last step in the biosynthesis of aliphatic glucosinolate core structures. cf. EC 2.8.2.24, aromatic desulfoglucosinolate sulfotransferase.
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Word Map
- 2.8.2.38
-
sulfotransferases
-
ecotypes
- paps
- 3'-phosphoadenosine
- cabbage
- brassica
-
non-radioactive
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heynh
-
cosubstrate
- broccoli
- jasmonate
-
ugt74b1
-
planta
- 5'-phosphate
- sinigrin
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
atsot18, sot18, ds-gl sot, sot17, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfotransferase
AtSOT18
cytosolic sulfotransferase 18
desulfo-glucosinolate sulfotransferase
ds-Gl SOT
SOT17
SOT18
3'-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfotransferase
UniProt
3'-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfotransferase
UniProt
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SOT17
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-
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-
SOT18
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + an aliphatic desulfoglucosinolate = adenosine 3',5'-bisphosphate + an aliphatic glucosinolate
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfotransferase
The enzyme catalyses the last step in the biosynthesis of aliphatic glucosinolate core structures. cf. EC 2.8.2.24, aromatic desulfoglucosinolate sulfotransferase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + 3-methylthiopropyl desulfoglucosinolate
adenosine 3',5'-bisphosphate + 3-methylthiopropyl glucosinolate
3'-phosphoadenylyl sulfate + desulfo-2-phenylethyl glucosinolate
adenosine 3',5'-bisphosphate + 2-phenylethyl glucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-3-butenylglucosinolate
adenosine 3',5'-bisphosphate + 3-butenylglucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-3-methylthiopropyl glucosinolate
adenosine-3',5'-bisphosphate + 3-methylthiopropyl glucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-3-methylthiopropylglucosinolate
adenosine 3',5'-bisphosphate + 3-methylthiopropylglucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-4-methylthiobutyl glucosinolate
adenosine-3',5'-bisphosphate + 4-methylthiobutyl glucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-4-methylthiobutylglucosinolate
adenosine 3',5'-bisphosphate + 4-methylthiobutylglucosinolate
3'-phosphoadenylyl sulfate + desulfo-5-methylthiopentylglucosinolate
adenosine 3',5'-bisphosphate + 5-methylthiopentylglucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-6-methylthiohexylglucosinolate
adenosine 3',5'-bisphosphate + 6-methylthiohexylglucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-7-methylthioheptyl glucosinolate
adenosine-3',5'-bisphosphate + 7-methylthioheptyl glucosinolate
3'-phosphoadenylyl sulfate + desulfo-7-methylthioheptylglucosinolate
adenosine 3',5'-bisphosphate + 7-methylthioheptylglucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-8-methylthiooctyl glucosinolate
adenosine-3',5'-bisphosphate + 8-methylthiooctyl glucosinolate
3'-phosphoadenylyl sulfate + desulfo-8-methylthiooctylglucosinolate
adenosine 3',5'-bisphosphate + 8-methylthiooctylglucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-benzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-indol-3-yl-methyl glucosinolate
adenosine-3',5'-bisphosphate + indol-3-yl-methyl glucosinolate
3'-phosphoadenylyl sulfate + desulfo-indole-3-methylglucosinolate
adenosine 3',5'-bisphosphate + indole-3-methylglucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
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-
-
?
adenosine 3',5'-bisphosphate + 7-methylthioheptyl glucosinolate
3'-phosphoadenylyl sulfate + 7-methylthioheptyl desulfoglucosinolate
adenosine 3',5'-bisphosphate + 8-methylthiooctyl glucosinolate
3'-phosphoadenylyl sulfate + 8-methylthiooctyl desulfoglucosinolate
adenosine 3',5'-bisphosphate + sinigrin
3'-phosphoadenylyl sulfate + desulfosinigrin
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
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?
3'-phosphoadenylyl sulfate + 3-methylthiopropyl desulfoglucosinolate
adenosine 3',5'-bisphosphate + 3-methylthiopropyl glucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + 3-methylthiopropyl desulfoglucosinolate
adenosine 3',5'-bisphosphate + 3-methylthiopropyl glucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-4-methylthiobutylglucosinolate
adenosine 3',5'-bisphosphate + 4-methylthiobutylglucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-4-methylthiobutylglucosinolate
adenosine 3',5'-bisphosphate + 4-methylthiobutylglucosinolate
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-
-
?
3'-phosphoadenylyl sulfate + desulfo-7-methylthioheptyl glucosinolate
adenosine-3',5'-bisphosphate + 7-methylthioheptyl glucosinolate
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-
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?
3'-phosphoadenylyl sulfate + desulfo-7-methylthioheptyl glucosinolate
adenosine-3',5'-bisphosphate + 7-methylthioheptyl glucosinolate
preferred substrate of isozyme SOT18 of ecotype C24
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-
?
3'-phosphoadenylyl sulfate + desulfo-8-methylthiooctyl glucosinolate
adenosine-3',5'-bisphosphate + 8-methylthiooctyl glucosinolate
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?
3'-phosphoadenylyl sulfate + desulfo-8-methylthiooctyl glucosinolate
adenosine-3',5'-bisphosphate + 8-methylthiooctyl glucosinolate
preferred substrate of isozyme SOT18 of ecotype C24
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?
3'-phosphoadenylyl sulfate + desulfo-indol-3-yl-methyl glucosinolate
adenosine-3',5'-bisphosphate + indol-3-yl-methyl glucosinolate
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?
3'-phosphoadenylyl sulfate + desulfo-indol-3-yl-methyl glucosinolate
adenosine-3',5'-bisphosphate + indol-3-yl-methyl glucosinolate
preferred substrate of isozyme SOT16 of ecotype C24
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-
?
3'-phosphoadenylyl sulfate + desulfosinigrin
adenosine 3',5'-bisphosphate + sinigrin
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-
-
?
3'-phosphoadenylyl sulfate + desulfosinigrin
adenosine 3',5'-bisphosphate + sinigrin
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-
-
?
adenosine 3',5'-bisphosphate + 7-methylthioheptyl glucosinolate
3'-phosphoadenylyl sulfate + 7-methylthioheptyl desulfoglucosinolate
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?
adenosine 3',5'-bisphosphate + 7-methylthioheptyl glucosinolate
3'-phosphoadenylyl sulfate + 7-methylthioheptyl desulfoglucosinolate
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?
adenosine 3',5'-bisphosphate + 8-methylthiooctyl glucosinolate
3'-phosphoadenylyl sulfate + 8-methylthiooctyl desulfoglucosinolate
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?
adenosine 3',5'-bisphosphate + 8-methylthiooctyl glucosinolate
3'-phosphoadenylyl sulfate + 8-methylthiooctyl desulfoglucosinolate
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?
adenosine 3',5'-bisphosphate + glucoiberverin
?
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?
additional information
?
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qualitative glucosinolate analysis in leaves of ecotype C24, overview
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?
additional information
?
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qualitative glucosinolate analysis in leaves of ecotype C24, overview
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?
additional information
?
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qualitative glucosinolate analysis in leaves of ecotype C24, overview
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?
additional information
?
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qualitative glucosinolate analysis in leaves of ecotype C24, overview
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?
additional information
?
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ecotype C24 isozyme SOT18 prefers the long-chain desulfoglucosinolates, 7-methylthioheptyl and 8-methylthiooctyl, derived from methionine. The substrate specificty of the isozyme SOT18 from ecotype Columbia-0 differs from the SOT18 from ecotype C24, detailed overview. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme SOT18 prefers the long-chain desulfoglucosinolates, 7-methylthioheptyl and 8-methylthiooctyl, derived from methionine. The substrate specificty of the isozyme SOT18 from ecotype Columbia-0 differs from the SOT18 from ecotype C24, detailed overview. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme SOT18 prefers the long-chain desulfoglucosinolates, 7-methylthioheptyl and 8-methylthiooctyl, derived from methionine. The substrate specificty of the isozyme SOT18 from ecotype Columbia-0 differs from the SOT18 from ecotype C24, detailed overview. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme SOT18 prefers the long-chain desulfoglucosinolates, 7-methylthioheptyl and 8-methylthiooctyl, derived from methionine. The substrate specificty of the isozyme SOT18 from ecotype Columbia-0 differs from the SOT18 from ecotype C24, detailed overview. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme substrate specificities: isozyme SOT17 shows an increased specific activity with increasing chain length of desulfoglucosinolates derived from methionine. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme substrate specificities: isozyme SOT17 shows an increased specific activity with increasing chain length of desulfoglucosinolates derived from methionine. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme substrate specificities: isozyme SOT17 shows an increased specific activity with increasing chain length of desulfoglucosinolates derived from methionine. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme substrate specificities: isozyme SOT17 shows an increased specific activity with increasing chain length of desulfoglucosinolates derived from methionine. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme substrate specificities: preference of isozyme SOT16 for the indolic desulfoglucosinolate indol-3-yl-methylglucosinolate. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme substrate specificities: preference of isozyme SOT16 for the indolic desulfoglucosinolate indol-3-yl-methylglucosinolate. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme substrate specificities: preference of isozyme SOT16 for the indolic desulfoglucosinolate indol-3-yl-methylglucosinolate. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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ecotype C24 isozyme substrate specificities: preference of isozyme SOT16 for the indolic desulfoglucosinolate indol-3-yl-methylglucosinolate. Substrate synthesis and optimization of the enzyme assay method, overview
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?
additional information
?
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enzyme AtSOT18 prefers the long-chain ds-Gls 7-methylthioheptyl Gl and 8-methylthiooctyl Gl (8MTO), that are also derived from methionine
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additional information
?
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enzyme AtSOT18 prefers the long-chain ds-Gls 7-methylthioheptyl Gl and 8-methylthiooctyl Gl (8MTO), that are also derived from methionine
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-
additional information
?
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usage of 3'-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfotransferase from Arabidopsis thaliana ecotype Col-0 and myrosinase from Brevicoryne brassicae for the biosynthesis of benzyl isothiocyanate by the combined expression of the optimized enzymes in vitro, product identity is confirmed by gas chromatography/mass spectrometry analysis. SOTs from different Arabidopsis ecotypes show different efficiencies
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additional information
?
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usage of 3'-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfotransferase from Arabidopsis thaliana ecotype Col-0 and myrosinase from Brevicoryne brassicae for the biosynthesis of benzyl isothiocyanate by the combined expression of the optimized enzymes in vitro, product identity is confirmed by gas chromatography/mass spectrometry analysis. SOTs from different Arabidopsis ecotypes show different efficiencies
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additional information
?
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enzyme AtSOT18 prefers the long-chain ds-Gls 7-methylthioheptyl Gl and 8-methylthiooctyl Gl (8MTO), that are also derived from methionine
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additional information
?
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enzyme prefers long-chained methionine-derived desulfoglucosinolates desulfo4-methythiobutylglucosinolate and desulfo-5-methylthiopentylglucosinoate
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?
additional information
?
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enzyme prefers long-chained methionine-derived desulfoglucosinolates desulfo4-methythiobutylglucosinolate and desulfo-5-methylthiopentylglucosinoate
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + desulfosinigrin
adenosine 3',5'-bisphosphate + sinigrin
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-
-
?
3'-phosphoadenylyl sulfate + desulfosinigrin
adenosine 3',5'-bisphosphate + sinigrin
-
-
-
?
additional information
?
-
qualitative glucosinolate analysis in leaves of ecotype C24, overview
-
-
?
additional information
?
-
qualitative glucosinolate analysis in leaves of ecotype C24, overview
-
-
?
additional information
?
-
qualitative glucosinolate analysis in leaves of ecotype C24, overview
-
-
?
additional information
?
-
-
qualitative glucosinolate analysis in leaves of ecotype C24, overview
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.055
desulfo-3-methylthiopropylglucosinolate
pH 9.0, 37°C, isozyme SOT18, ecotype Columbia-0
0.07
desulfo-3-methylthiopropylglucosinolate
pH 9.0, 37°C, isozyme SOT16
0.088
desulfo-3-methylthiopropylglucosinolate
pH 9.0, 37°C, isozyme SOT17
0.1
desulfo-3-methylthiopropylglucosinolate
pH 9.0, 37°C, isozyme SOT18, ecotype C24
0.043
desulfo-4-methylthiobutylglucosinolate
pH 9.0, 37°C, isozyme SOT18, ecotype Columbia-0
0.065
desulfo-4-methylthiobutylglucosinolate
pH 9.0, 37°C, isozyme SOT17
0.08
desulfo-4-methylthiobutylglucosinolate
pH 9.0, 37°C, isozyme SOT16
0.13
desulfo-4-methylthiobutylglucosinolate
pH 9.0, 37°C, isozyme SOT18, ecotype C24
additional information
additional information
kinetics, overview
-
additional information
additional information
kinetics, overview
-
additional information
additional information
kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
inhibition kinetics
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0073
recombinant mutant T96A, substrate 3-methylthiopropyl desulfoglucosinolate, pH 8.0, 37°C
0.028
recombinant mutant P136A, substrate glucobrassicin, pH 8.0, 37°C
0.03
recombinant wild-type enzyme, substrate glucobrassicin, pH 8.0, 37°C
0.032
recombinant mutant T96A, substrate 8-methylthiooctyl desulfoglucosinolate, pH 8.0, 37°C
0.053
recombinant wild-type enzyme, substrate sinigrin, pH 8.0, 37°C
0.0971
recombinant wild-type enzyme, substrate 8-methylthiooctyl desulfoglucosinolate, pH 8.0, 37°C
0.0974
recombinant wild-type enzyme, substrate 3-methylthiopropyl desulfoglucosinolate, pH 8.0, 37°C
0.104
recombinant mutant P136A, substrate 3-methylthiopropyl desulfoglucosinolate, pH 8.0, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype C24 and ecotype Col0 differ in exchanges D301G and K339N
UniProt
brenda
ecotype C24 and ecotype Col0 differ in exchanges W183R and S344T
UniProt
brenda
isozyme SOT18; ecotypes C24 and Columbia-0, isozyme SOT18
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
low expression in plants up to 4 weeks old and slightly elevated in the oldest plants harvested in weeks 5 and 6
brenda
mature leaf of the primary rosette, high expression
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
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
evolution
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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
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