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Information on EC 2.8.2.24 - aromatic desulfoglucosinolate sulfotransferase
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EC Tree
2.8.2.24 aromatic desulfoglucosinolate sulfotransferaseIUBMB Comments
This enzyme, characterized from cruciferous plants, catalyses the last step in the biosynthesis of tryptophan- and phenylalanine-derived glucosinolates. cf. EC 2.8.2.38, aliphatic desulfoglucosinolate sulfotransferase.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
sot16, 3'-phosphoadenosine-5'-phosphosulfate:desulfoglucosinolate sulfotransferase, desulfoglucosinolate:paps sulfotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-phosphoadenosine-5'-phosphosulfate:desulfoglucosinolate sulfotransferase
-
-
-
-
desulfoglucosinolate:PAPS sulfotransferase
PAPS-desulfoglucosinolate sulfotransferase
-
-
-
-
SOT16
sulfotransferase, desulfoglucosinolate
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + desulfoglucotropeolin = adenosine 3',5'-bisphosphate + glucotropeolin
3'-phosphoadenylyl sulfate + indolylmethyl-desulfoglucosinolate = adenosine 3',5'-bisphosphate + glucobrassicin
(2)
-
-
-
3'-phosphoadenylyl sulfate + desulfoglucotropeolin = adenosine 3',5'-bisphosphate + glucotropeolin
mechanism
-
3'-phosphoadenylyl sulfate + desulfoglucotropeolin = adenosine 3',5'-bisphosphate + glucotropeolin
(1)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:aromatic desulfoglucosinolate sulfotransferase
This enzyme, characterized from cruciferous plants, catalyses the last step in the biosynthesis of tryptophan- and phenylalanine-derived glucosinolates. cf. EC 2.8.2.38, aliphatic desulfoglucosinolate sulfotransferase.
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CAS REGISTRY NUMBER
COMMENTARY
121479-85-4
-
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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'-phosphoadenosine-5'-phosphosulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
-
-
-
?
3'-phosphoadenylyl sulfate + desulfo-p-hydroxy-benzylglucosinolate
adenosine 3',5'-bisphosphate + p-hydroxy-benzylglucosinolate
-
-
-
-
?
3'-phosphoadenylyl sulfate + desulfoallylglucosinolate
adenosine 3',5'-bisphosphate + allylglucosinolate
-
-
-
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
3'-phosphoadenylylsulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
i.e. 3'-phosphoadenosine 5'phosphosulfate, i.e. PAPS
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylyl sulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
absolute specificity for desulfoglucosinolate structure
-
?
3'-phosphoadenylylsulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
-
-
-
?
3'-phosphoadenylylsulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
-
-
?
additional information
?
-
analysis/evaluation of desulfoglucosinolate:PAPS 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
-
-
-
additional information
?
-
analysis/evaluation of desulfoglucosinolate:PAPS 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
?
-
-
no activity with adenosine-5'-phosphosulfate as donor
-
-
?
additional information
?
-
-
involved in the biosynthesis of glucosinolates
-
-
?
additional information
?
-
-
involved with EC 2.4.1.195 in final steps of thioglycoside biosynthesis in cruciferous plants
-
-
?
additional information
?
-
-
involved with EC 2.4.1.195 in final steps of thioglycoside biosynthesis in cruciferous plants
-
-
?
additional information
?
-
-
no acceptors are quercetin, rutin, kaempferol, p-coumaric acid, ferulic acid, caffeic acid, phenylacetaldoxime
-
-
?
additional information
?
-
-
involved in the biosynthesis of glucosinolates
-
-
?
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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'-phosphoadenylylsulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
3'-phosphoadenylylsulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
-
-
-
?
3'-phosphoadenylylsulfate + desulfobenzylglucosinolate
adenosine 3',5'-bisphosphate + benzylglucosinolate
-
-
-
?
additional information
?
-
-
involved in the biosynthesis of glucosinolates
-
-
?
additional information
?
-
-
involved with EC 2.4.1.195 in final steps of thioglycoside biosynthesis in cruciferous plants
-
-
?
additional information
?
-
-
involved with EC 2.4.1.195 in final steps of thioglycoside biosynthesis in cruciferous plants
-
-
?
additional information
?
-
-
involved in the biosynthesis of glucosinolates
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine-3',5'-bisphosphate
-
competitive to 3'-phosphoadenylylsulfate, kinetics
additional information
-
no inhibition by 3'-AMP, 5'-AMP, 2',5'-AMP, 3',5'-cAMP, 5'-ADP, 5'-ATP, adenosine-5'-phosphosulfate, benzaldoxime, phenylacetohydroximate, phenylacetothiohydroximate, S-methylphenylacetothiohydroximate, benzylglucosinolate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
3'-phosphoadenosine-5'-phosphosulfate
-
isoenzyme AtSOT18 Co10, pH 9.0, 37°C
0.1
3'-phosphoadenosine-5'-phosphosulfate
-
isoenzyme AtSOT16 C24, pH 9.0, 37°C
0.1
3'-phosphoadenosine-5'-phosphosulfate
-
isoenzyme AtSOT17 C24, pH 9.0, 37°C
additional information
additional information
-
not detectable: 3'-phosphoadenosine-5'-phosphosulfate, isoenzyme AtSOT18 C24, pH 9.0, 37°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
0.0016197 Vmax desulfobenzylglucosinolate, isoenzyme AtSOT18 C24, pH 9.0, 37°C
additional information
-
0.007499 Vmax 3'-phosphoadenosine-5'-phosphosulfate, isoenzyme AtSOT17 C24, pH 9.0, 37°C
additional information
-
0.008518 Vmax desulfobenzylglucosinolate, isoenzyme AtSOT17 C24, pH 9.0, 37°C
additional information
-
0.01026 Vmax 3'-phosphoadenosine-5'-phosphosulfate, isoenzyme AtSOT18 C24, pH 9.0, 37°C
additional information
-
0.0415 Vmax desulfobenzylglucosinolate, isoenzyme AtSOT16 C24, pH 9.0, 37°C
additional information
-
0.05105 Vmax 3'-phosphoadenosine-5'-phosphosulfate, isoenzyme AtSOT18 Co10, pH 9.0, 37°C
additional information
-
0.05159 Vmax desulfobenzylglucosinolate, isoenzyme AtSOT18 Co10, pH 9.0, 37°C
additional information
-
0.06599 Vmax 3'-phosphoadenosine-5'-phosphosulfate, isoenzyme AtSOT16 C24, pH 9.0, 37°C
additional information
-
isoenzyme AtSOT16 C24 best substrate: 2-phenylethyl-glucosinolate
additional information
-
isoenzyme AtSOT17 C24 best substrate: benzylglucosinolate
additional information
-
isoenzyme AtSOT18 C24 best substrate: 6-methylthiohexylglucosinolate
additional information
-
isoenzyme AtSOT18 Co10 best substrate: benzylglucosinolate
additional information
-
isoenzyme AtSOT18G301D best substrate: 4-methylthiobutylglucosinolate
additional information
-
isoenzyme AtST5a: best substrate: indole-3-methyl-desulfoglucosinolate, other substrates: benzyl-desulfoglucosinolate, 4-methylthiobutyl-desulfoglucosinolate, 4-methoxyindole-3-methyl-desulfoglucosinolate, N-methoxyindole-3-methyl-desulfoglucosinolate. pH 7.0, 30°C
additional information
-
isoenzyme AtST5b: best substrate: 7-methylthioheptyl-desulfoglucosinolate, other substrates: 8-methylthiooctyl-desulfoglucosinolate, 4-methylthiobutyl-desulfoglucosinolate, benzyl-desulfoglucosinolate, indole-3-methyl-desulfoglucosinolate, 8-methylsulfinyloctyl-desulfoglucosinolate, 3-butenyl-desulfoglucosinolate. pH 7.0, 30°C
additional information
-
isoenzyme AtST5c: best substrate: 8-methylthiooctyl-desulfoglucosinolate, other substrates: 7-methylthioheptyl-desulfoglucosinolate, benzyl-desulfoglucosinolate, 3-butenyl-desulfoglucosinolate, 4-methylthiobutyl-desulfoglucosinolate, 8-methylsulfinyloctyl-desulfoglucosinolate, 4-methylsulfinylbutyl-desulfoglucosinolate. pH 7.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 40
-
about 85% of maximal activity at 25°C and about half-maximal activity at 40°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
expression of the gene paralogues is not tissue-specific but varies greatly depending on the tissue type. The expression is also developmentally regulated for some paralogues but not for others
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
the enzyme is involved in the glucosinolate biosynthesis pathway, glucosinolates play important roles in plant defense against herbivores and microbes, as well as in human nutrition
metabolism
-
the enzyme is involved in the glucosinolate biosynthesis pathway, glucosinolates play important roles in plant defense against herbivores and microbes, as well as in human nutrition
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SOT16_ARATH
338
0
39219
Swiss-Prot
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G301D
-
isoenzyme AtSOT18 C24, 25times higher specific activity with desulfobenzylglucosinolate
additional information
additional information
generation of two chimeric cytochrome P450 enzymes from CYP79A2 and CYP83B1 are constructed and attempted to be functionally expressed in Escherichia coli strain BL21(DE3). The Escherichia coli cystathionine beta-lyase is used to replace the plant-derived CS lyase whose active form cannot be expressed in Escherichia coli. Recomstruction of the BITC biosynthesis pathway from plants in the bacteria, involving CYP79A2 and CYP83B1, and the glutathione S-transferase, gamma-glutamyl peptidase, C-S lyase, glucosyltransferase, desulfoglucosinolate:PAPS sulfotransferase, and myrosinase are encoded by genes GSTF, GGP1, SUR1, UGT74B1, SOT16, and MYR, respectively, overview. Expression of codon-optimized sulfotransferase gene SOT16 from Arabidopsis thaliana fails because of the formation of inclusion bodies, SOT16 is successfully replaced for SOT18 (EC 2.8.2.38)
additional information
-
generation of two chimeric cytochrome P450 enzymes from CYP79A2 and CYP83B1 are constructed and attempted to be functionally expressed in Escherichia coli strain BL21(DE3). The Escherichia coli cystathionine beta-lyase is used to replace the plant-derived CS lyase whose active form cannot be expressed in Escherichia coli. Recomstruction of the BITC biosynthesis pathway from plants in the bacteria, involving CYP79A2 and CYP83B1, and the glutathione S-transferase, gamma-glutamyl peptidase, C-S lyase, glucosyltransferase, desulfoglucosinolate:PAPS sulfotransferase, and myrosinase are encoded by genes GSTF, GGP1, SUR1, UGT74B1, SOT16, and MYR, respectively, overview. Expression of codon-optimized sulfotransferase gene SOT16 from Arabidopsis thaliana fails because of the formation of inclusion bodies, SOT16 is successfully replaced for SOT18 (EC 2.8.2.38)
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity loss due to instability at pH values near the isoelectric point 5.2
643824
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM Tris buffer, pH 7.5, 14 mM 2-mercaptoethanol, 10% glycerol, at least 2 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of the enzyme with myrosinase from Brevicoryne brassicae in Escherichia coli, expression of codon-optimized sulfotransferase gene SOT16 from Arabidopsis thaliana fails because of the formation of inclusion bodies
DNA and amino acid sequence determination and analysis, gene structure, phylogenetic tree, genomic study of genes involved in glucosinolate biosynthesis, comparison with Arabidopsis thaliana genome, overview
-
DNA and amino acid sequence determination and analysis, gene structure, phylogenetic tree, genomic study of genes involved in glucosinolate biosynthesis, comparison with Brassica rapa genome, overview
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jain, J.C.; Reed, D.W.; Groot Wassink, J.W.D.; Underhill, E.W.
A radioassay of enzymes catalyzing the glucosylation and sulfation steps of glucosinolate biosynthesis in Brassica species
Anal. Biochem.
178
137-140
1989
Brassica rapa subsp. oleifera, Brassica juncea, Brassica napus, Brassica nigra, Brassica oleracea
brenda
Jain, J.C.; Michayluk, M.R.; Groot Wassink, J.W.D.; Underhill, E.W.
Distribution of enzymes catalyzing the glycosylation and sulfation steps of glucosinolate biosynthesis in Brassica juncea seedlings and cultured cells
Plant Sci.
64
25-29
1989
Brassica juncea
-
brenda
Jain, J.C.; Groot Wassink, J.W.D.; Reed, D.W.; Underhill, E.W.
Persistent co-purification of enzymes catalyzing the sequential glucosylation and sulfation steps in glucosinolate biosynthesis
J. Plant Physiol.
136
356-361
1990
Brassica juncea
-
brenda
Glendening, T.M.; Poulton, J.E.
Partial purification and characterization of a 3'-phosphoadenosine 5'-phosphosulfate: desulfoglucosinolate sulfotransferase from cress (Lepidium sativum)
Plant Physiol.
94
811-816
1990
Arabidopsis thaliana, Brassica rapa subsp. oleifera, Lepidium sativum, Sinapis alba, Tropaeolum majus
brenda
Jain, J.C.; Groot Wassink, J.W.D.; Kolenovsky, A.D.; Underhill, E.W.
Purification and properties of 3'-phosphoadenosine 5'-phosphosulfate: desulphoglucosinolate sulphotransefrase from Brassica juncea cell cultures
Phytochemistry
29
1425-1428
1990
Brassica juncea
-
brenda
Klein, M.; Reichelt, M.; Gershenzon, J.; Papenbrock, J.
The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis have different substrate specificities and are differentially expressed
FEBS J.
273
122-136
2006
Arabidopsis thaliana
brenda
Piotrowski, M.; Schemenewitz, A.; Lopukhina, A.; Muller, A.; Janowitz, T.; Weiler, E.W.; Oecking, C.
Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana catalyze the final step in the biosynthesis of the glucosinolate core structure
J. Biol. Chem.
279
50717-50725
2004
Arabidopsis thaliana
brenda
Zang, Y.X.; Kim, H.U.; Kim, J.A.; Lim, M.H.; Jin, M.; Lee, S.C.; Kwon, S.J.; Lee, S.I.; Hong, J.K.; Park, T.H.; Mun, J.H.; Seol, Y.J.; Hong, S.B.; Park, B.S.
Genome-wide identification of glucosinolate synthesis genes in Brassica rapa
FEBS J.
276
3559-3574
2009
Arabidopsis thaliana, Brassica rapa
brenda
Liu, F.; Yang, H.; Wang, L.; Yu, B.
Biosynthesis of the high-value plant secondary product benzyl isothiocyanate via functional expression of multiple heterologous enzymes in Escherichia coli
ACS Synth. Biol.
5
1557-1565
2016
Arabidopsis thaliana (Q9C9D0), Arabidopsis thaliana Col-0 (Q9C9D0)
brenda
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