Any feedback?
Information on EC 2.8.2.9 - tyrosine-ester sulfotransferase
for references in articles please use BRENDA:EC2.8.2.9Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.8.2.9 tyrosine-ester sulfotransferaseIUBMB Comments
Phenols and organic hydroxylamines can act as acceptors (cf. EC 2.8.2.1 aryl sulfotransferase).
Specify your search results
Word Map
- 2.8.2.9
-
sults
- phenol
- pap
- steroid
- xenobiotics
- 3'-phosphoadenosine
- 5'-phosphosulfate
- dehydroepiandrosterone
-
glucuronidation
-
sulfatase
- 3'-phosphoadenosine-5'-phosphosulfate
- hydroxysteroids
- estradiol
-
udp-glucuronosyltransferase
- chondroitin
- heparan
- dheas
- estrone
-
drug-metabolizing
- p-nitrophenol
- pentachlorophenol
- sult1a3
-
sulfurylation
- n-hydroxy-2-acetylaminofluorene
-
sulfoconjugation
- minoxidil
-
arylamines
- 2-acetylaminofluorene
- l-selectin
- 2-naphthol
- 3'-phosphate
-
glucuronyltransferase
-
desulfated
- keratan
- pregnenolone
-
hepatocarcinogenicity
-
17beta-hydroxysteroid
-
monosulfate
-
2-amino-1-methyl-6-phenylimidazo4,5-bpyridine
-
n-hydroxy
-
35ssulfate
-
glucuronyl
-
32p-postlabeling
-
udp-glucuronosyl
- 4-sulfate
-
n-sulfation
- galactosylceramide
-
promutagens
-
3-o-sulfation
- tibolone
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
sulfotransferase, ast iv, aryl sulfotransferase iv, st1a1, sult1d1, tyrosine-ester sulfotransferase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aryl sulfotransferase IV
beta-aryl sulfotransferase IV
-
-
-
-
beta-AST IV
-
-
-
-
L-tyrosine methyl ester sulfotransferase
-
-
-
-
ST1A1
-
-
-
-
sulfotransferase, tyrosine ester
-
-
-
-
tyrosine ester sulfotransferase
-
-
-
-
aryl sulfotransferase IV
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + L-tyrosine methyl ester = adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate
3'-phosphoadenylyl sulfate + L-tyrosine methyl ester = adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate
mechanism
-
3'-phosphoadenylyl sulfate + L-tyrosine methyl ester = adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate
random rapid equilibrium bi bi kinetic mechanism
-
3'-phosphoadenylyl sulfate + L-tyrosine methyl ester = adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:L-tyrosine-methyl-ester sulfotransferase
Phenols and organic hydroxylamines can act as acceptors (cf. EC 2.8.2.1 aryl sulfotransferase).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9055-56-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(1S)-2-methyl-1-phenylpropan-1-ol
adenosine 3',5'-bisphosphate + (1S)-2-methyl-1-phenylpropyl sulfate
-
stereochemical configuration is important, the other enantiomer acts as inhibitor
-
-
?
3'-phosphoadenosine 5'-phosphosulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + (R)-(-)-1,2,3,4-tetrahydro-1-naphthol
adenosine 3',5'-bisphosphate + (R)-(-)-1,2,3,4-tetrahydro-1-naphthyl sulfate
-
activity is abserved with wild-type enzyme and mutant enzymes F77A, F138A and Y236A
-
-
?
3'-phosphoadenylylsulfate + (S)-(+)-1,2,3,4-tetrahydro-1-naphthol
adenosine 3',5'-bisphosphate + (S)-(+)-1,2,3,4-tetrahydro-1-naphthyl sulfate
-
mutant enzyme F77A and F138A show activity, wild-type enzyme and mutant enzyme Y236A show no activity
-
-
?
3'-phosphoadenylylsulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 2-chloro-4-nitrophenol
adenosine 3',5'-bisphosphate + 2-chloro-4-nitrophenyl sulfate
3'-phosphoadenylylsulfate + 2-chlorophenol
adenosine 3',5'-bisphosphate + 2-chlorophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 2-cyanoethyl-N-hydroxythioacetamide
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 2-cyanoethyl-N-hydroxythioacetimidate
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 2-fluoro-4-nitrophenol
adenosine 3',5'-bisphosphate + 2-fluoro-4-nitrophenyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 3-chlorophenol
adenosine 3',5'-bisphosphate + 3-chlorophenyl sulfate
3'-phosphoadenylylsulfate + 3-fluoro-4-nitrophenol
adenosine 3',5'-bisphosphate + 3-fluoro-4-nitrophenyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3-methoxy-4-hydroxyphenylglycol
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + 3-methylphenol
adenosine 3',5'-bisphosphate + 3-methylphenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 3-nitrophenol
adenosine 3',5'-bisphosphate + 3-nitrophenyl sulfate
3'-phosphoadenylylsulfate + 4-chlorophenol
adenosine 3',5'-bisphosphate + 4-chlorophenyl sulfate
3'-phosphoadenylylsulfate + 4-methoxyphenol
adenosine 3',5'-bisphosphate + 4-methoxyphenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-methylphenol
adenosine 3',5'-bisphosphate + 4-methylphenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-methylumbelliferol
adenosine 3',5'-bisphosphate + 4-methylumbelliferyl sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylylsulfate + 5-hydroxytryptamine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 5-hydroxytryptophol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 9-hydroxy-N-2-fluorenylacetamide
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + Ala-Tyr
adenosine 3',5'-bisphosphate + Ala-(O-sulfo)Tyr
-
-
-
-
?
3'-phosphoadenylylsulfate + Asp-Arg-Asp-Tyr-Met-Gly
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + caerulein
adenosine 3',5'-bisphosphate + ?
-
nonsulfated
-
-
?
3'-phosphoadenylylsulfate + cholecystokinin
adenosine 3',5'-bisphosphate + ?
-
nonsulfated
-
-
?
3'-phosphoadenylylsulfate + epinephrine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + GlyTyr
adenosine 3',5'-bisphosphate + Gly-(O-sulfo)Tyr
-
-
-
-
?
3'-phosphoadenylylsulfate + hydrocortisone
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + L-4-hydroxyphenylglycine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + L-tyrosine
adenosine 3',5'-bisphosphate + tyrosine O4-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + L-tyrosine allyl ester
adenosine 3',5'-bisphosphate + tyrosine allyl ester 4-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + L-tyrosine amide
adenosine 3',5'-bisphosphate + O-sulfo-L-tyrosine amide
3'-phosphoadenylylsulfate + L-tyrosine benzyl ester
adenosine 3',5'-bisphosphate + tyrosine benzyl ester 4-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + L-tyrosine ethyl ester
adenosine 3',5'-bisphosphate + tyrosine ethyl ester 4-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + L-tyrosine methyl ester
adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate
3'-phosphoadenylylsulfate + L-tyrosine tert-butyl ester
adenosine 3',5'-bisphosphate + tyrosine tert-butyl ester 4-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + methylphenol
adenosine 3',5'-bisphosphate + methylphenyl sulfate
-
3-methylphenol or 4-methylphenol
-
-
?
3'-phosphoadenylylsulfate + N-acetyl-L-tyrosine ethyl ester
adenosine 3',5'-bisphosphate + N-acetyl-L-tyrosine O4-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + N-acetylserotonin
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + N-ethyl-N-hydroxyaniline
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + N-hydroxy-N-ethylaniline
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + N-hydroxy-N-methylaniline
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + N-hydroxy-N-n-propylaniline
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + nitrophenol
adenosine 3',5'-bisphosphate + nitrophenyl sulfate
3'-phosphoadenylylsulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + serotonin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + tert-butoxycarbonyl-Asp-Arg-Asp-Tyr-Met-Gly
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + tert-butoxycarbonyl-Asp-Tyr
adenosine 3',5'-bisphosphate + tert-butoxycarbonyl-Asp-Tyr-O4-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + tert-butoxycarbonyl-Asp-Tyr-Met
adenosine 3',5'-bisphosphate + tert-butoxycarbonyl-Asp-Tyr-(O4-sulfate)-Met
-
-
-
-
?
3'-phosphoadenylylsulfate + tert-butoxycarbonyl-Asp-Tyr-Met-Gly
adenosine 3',5'-bisphosphate + tert-butoxycarbonyl-Asp-Tyr-(O4-sulfate)-Met-Gly
-
-
-
-
?
3'-phosphoadenylylsulfate + tert-butoxycarbonyl-Asp-Tyr-Met-Gly-Trp
adenosine 3',5'-bisphosphate + tert-butoxycarbonyl-Asp-Tyr-(O4-sulfate)-Met-Gly-Trp
-
-
-
-
?
3'-phosphoadenylylsulfate + tert-butoxycarbonyl-Asp-Tyr-Met-Gly-Trp-Met
adenosine 3',5'-bisphosphate + tert-butoxycarbonyl-Asp-Tyr-(O4-sulfate)-Met-Gly-Trp-Met
-
-
-
-
?
3'-phosphoadenylylsulfate + tert-butoxycarbonyl-Asp-Tyr-Met-Gly-Trp-Met-Asp-Phe-NH2
adenosine 3',5'-bisphosphate + tert-butoxycarbonyl-Asp-Tyr-(O4-sulfate)-Met-Gly-Trp-Met-Asp-Phe-NH2
-
i.e. Boc-CCK-8 ns
-
-
?
3'-phosphoadenylylsulfate + tert-butoxycarbonylcholecystokinin-octapeptide
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + tyramine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + TyrGly
adenosine 3',5'-bisphosphate + 4O-sulfo-Tyr-Gly
-
-
-
-
?
adenosine 3'-phosphate 5'-sulfophosphate + L-tyrosine methyl ester
?
-
-
-
-
?
R-(-)-1,2,3,4-tetrahydro-1-naphthol
adenosine 3',5'-bisphosphate + (R)-(-)-1,2,3,4-tetrahydro-1-naphthyl sulfate
-
stereochemical configuration is important, the other enantiomer acts as inhibitor
-
-
?
3'-phosphoadenylylsulfate + 2-chloro-4-nitrophenol
adenosine 3',5'-bisphosphate + 2-chloro-4-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 2-chloro-4-nitrophenol
adenosine 3',5'-bisphosphate + 2-chloro-4-nitrophenyl sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 3-chlorophenol
adenosine 3',5'-bisphosphate + 3-chlorophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 3-chlorophenol
adenosine 3',5'-bisphosphate + 3-chlorophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 3-methoxy-4-hydroxyphenylglycol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 3-methoxy-4-hydroxyphenylglycol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 3-nitrophenol
adenosine 3',5'-bisphosphate + 3-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 3-nitrophenol
adenosine 3',5'-bisphosphate + 3-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-chloro-N-hydroxyaniline
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-chloro-N-hydroxyaniline
adenosine 3',5'-bisphosphate + ?
-
oxidative degradation N-hydroxyaniline causes inhibition
-
-
?
3'-phosphoadenylylsulfate + 4-chloro-N-hydroxyaniline
adenosine 3',5'-bisphosphate + ?
-
oxidative degradation N-hydroxyaniline causes inhibition
-
-
?
3'-phosphoadenylylsulfate + 4-chlorophenol
adenosine 3',5'-bisphosphate + 4-chlorophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-chlorophenol
adenosine 3',5'-bisphosphate + 4-chlorophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + L-tyrosine amide
adenosine 3',5'-bisphosphate + O-sulfo-L-tyrosine amide
-
-
-
-
?
3'-phosphoadenylylsulfate + L-tyrosine amide
adenosine 3',5'-bisphosphate + O-sulfo-L-tyrosine amide
-
-
-
-
?
3'-phosphoadenylylsulfate + L-tyrosine methyl ester
adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + L-tyrosine methyl ester
adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + N-hydroxy-2-aminofluorene
adenosine 3',5'-bisphosphate + ?
-
causes inhibition under reaction conditions where oxidative degradation occurs
-
-
?
3'-phosphoadenylylsulfate + N-hydroxy-2-aminofluorene
adenosine 3',5'-bisphosphate + ?
-
causes inhibition under reaction conditions where oxidative degradation occurs
-
-
?
3'-phosphoadenylylsulfate + N-hydroxyaniline
adenosine 3',5'-bisphosphate + ?
-
oxidative degradation of N-hydroxyaniline causes inhibition
-
-
?
3'-phosphoadenylylsulfate + N-hydroxyaniline
adenosine 3',5'-bisphosphate + ?
-
oxidative degradation of N-hydroxyaniline causes inhibition
-
-
?
3'-phosphoadenylylsulfate + nitrophenol
adenosine 3',5'-bisphosphate + nitrophenyl sulfate
-
3-nitrophenol or 4-nitrophenol
-
-
?
3'-phosphoadenylylsulfate + nitrophenol
adenosine 3',5'-bisphosphate + nitrophenyl sulfate
-
3-nitrophenol or 4-nitrophenol
-
-
?
additional information
?
-
no substrate for isozymes HAST4 and HAST4v: dopamine
-
-
?
additional information
?
-
-
no substrate for isozymes HAST4 and HAST4v: dopamine
-
-
?
additional information
?
-
-
forms sulfuric acid esters from a wide range of phenols, tyrosine carboxyesters, catechols, benzylic alcohols, arylhydroxamic acids and N-hydroxy arylamines. Stereochemical configuration of chiral benzyclic alcohols is an important factor in substrate specificity. One enantiomer may act as substrate, the other as inhibitor
-
-
?
additional information
?
-
-
natural enzyme acts best with naphthylamine at an acidic pH and the recombinant enzyme best at high pH values
-
-
?
additional information
?
-
-
transfer of a sulfuryl group to an aryl hydroxyl group
-
-
?
additional information
?
-
-
involved in the sulfation of physiologically active amines
-
-
?
additional information
?
-
-
enzyme is specific for substrate molecules with a free and unprotonated amino group and an unionized hydroxyl group
-
-
?
additional information
?
-
-
catalyzes sulfate ester formation with simple phenols at an acidic pH and with several physiological metabolites at a more alkaline pH
-
-
?
additional information
?
-
-
active with phenols, hydroxylamines and esters of tyrosine
-
-
?
additional information
?
-
-
it appears unlikely that the enzyme is involved in the biosynthesis of proteins containing L-tyrosine O-sulfate residues, it is probably important in sulfation of physiologically active amines
-
-
?
additional information
?
-
-
the enzyme is involved in detoxification and is susceptible to downregulation by hepatotoxic xenobiotics, overview
-
-
?
additional information
?
-
-
forms sulfuric acid esters from a wide range of phenols, tyrosine carboxyesters, catechols, benzylic alcohols, arylhydroxamic acids and N-hydroxy arylamines. Stereochemical configuration of chiral benzyclic alcohols is an important factor in substrate specificity. One enantiomer may act as substrate, the other as inhibitor
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
additional information
?
-
-
it appears unlikely that the enzyme is involved in the biosynthesis of proteins containing L-tyrosine O-sulfate residues, it is probably important in sulfation of physiologically active amines
-
-
?
additional information
?
-
-
the enzyme is involved in detoxification and is susceptible to downregulation by hepatotoxic xenobiotics, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-naphthylacetic acid
-
competitive with respect to 1-naphththalenemethanol
2'-O-[(R)-formyl(adenin-9-yl)methyl]-(S)-glyceraldehyde 3'-triphosphate
-
ATPDA, irreversible, inhibition prevented by either adenosine 3,5'-diphosphate or 3'-phosphoadenylylsulfate, binds to Lys65 and Cys66 at the PAPS binding site
2-acetylaminofluorene
-
increases and/or alters the inhibitory effect of metal ions, relationship between inhibition by heavy metal ions and dietary 2-acetylaminofluorene, overview
2-naphthylacetic acid
-
competitive with respect to 1-naphththalenemethanol
Cd2+
-
strong inhibition in vitro and in vivo, 50% inhibition of purified enzyme at about 0.0025 mM, 50% inhibition in liver cytosol at about 0.025 mM
Cu2+
-
elevated copper levels in the diet result in reduced enzyme levels in rat liver, strong inhibition in vitro and in vivo, 50% inhibition of purified enzyme at about 0.0025 mM, 50% inhibition in liver cytosol at about 0.025 mM
iodoacetamide
-
pH 7.5, 30°C, inhibition prevented by presence of 3'-phosphate 5'-sulfatophosphate but not by L-tyrosine methyl ester
N-Hydroxy-2-acetylaminofluorene
-
N-OH-2AAF, formation of AST IV:2AAF adducts leads to irreversible inactivation
N-hydroxy-2-aminofluorene
-
N-OH-2AF, causes inhibition under reaction conditions where oxidative degradation occurs
N-hydroxyaniline
-
causes inhibition under reaction conditions where oxidative degradation occurs, activity rapidly decreases to less than 10% of the initial activity
R-(+)-2-methyl-1-phenylpropanol
-
competitive, reversible inhibitor, stereochemical configuration is important, the other enantiomer acts as substrate
S-(+)-1,2,3,4-tetrahydro-1-naphthol
-
competitive, reversible inhibitor, stereochemical configuration is important, the other enantiomer acts as substrate
Zn2+
-
indirect inhibition mechanism, strong inhibition in vitro and in vivo, 50% inhibition of purified enzyme at about 0.0025 mM, 50% inhibition in liver cytosol at about 0.025 mM
2,6-Dichloro-4-nitrophenol
50% inhibition of HAST4 at 0.005 mM; 50% inhibition of HAST4v at 0.02 mM
4-chloro-N-hydroxyaniline
-
causes inhibition under reaction conditions where oxidative degradation occurs
adenosine 3',5'-bisphosphate
-
PAP, competitive to 3'-phosphoadenylylsulfate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activates, degree of activation is more marked with preparations previously stored at 0°C or -10°C
5,5'-dithiobis(2-nitrobenzoate)
-
low concentrations lead to increase of activity at a physiological pH, higher concentrations lead to complete inactivation
Diamide
-
low concentrations lead to increase of activity at a physiological pH, higher concentrations lead to complete inactivation
dithiothreitol
-
activates, degree of activation is more marked with preparations previously stored at 0°C or -10°C
glutathione
-
activates, degree of activation is more marked with preparations previously stored at 0°C or -10°C
glutathione disulfide
-
leads to the formation of internal disulfide bonds between Cys66 and Cys232, activates the enzyme and allows it to function at a pH optimum in the physiological range
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
2'-O-[(R)-formyl(adenin-9-yl)methyl]-(S)-glyceraldehyde 3'-triphosphate
-
pH 7, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.8 - 1
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6
-
two optima: pH 6 and pH 9.7, reduced enzyme activity with 2-naphthylamine as substrate
9.7
-
two optima: pH 6 and pH 9.7, reduced activity with 2-naphthylamine as substrate
additional information
5.5
-
2-naphthol, no formation of sulfate esters from tyrosine methyl ester, epinephrine, octopamine, tyramine, serotonin, N-acetylserotonin
additional information
-
natural enzyme acts best with naphthylamine at an acidic pH and the recombinant enzyme best at high pH values
additional information
-
pH optima for sulfation are dependent on the oxidation state of the sulfotransferase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
5.8
-
pH gradient from pH 3.5 to pH 10 in a linear sucrose gradient from 5% to 40%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the activity of aryl sulfotransferase IV increases 3fold to 8fold in lungs treated with more than 95% O2. However, hyperoxic exposure does not change the mRNA and protein levels of aryl sulfotransferase IV in lungs. Oxidative regulation occurs at the level of protein modification
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). ST1A2_HUMAN
295
0
34310
Swiss-Prot
other Location (Reliability: 5)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33500
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
oxidative regulation of aryl sulfotransferase IV is not caused by dimer-monomer status change
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
oxidative regulation occurs at the level of protein modification. Active site Cys chemical modification can regulate AST IV activity both in vivo and in vitro
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SULT1D1 complexed with 3'-phosphoadenosine-5'-phosphate plus 4-nitrophenol or 3'-phosphoadenosine-5'-phosphate plus 1-naphthol, hanging drop vapor diffusion method, using 16% (w/v) PEG 10000, 10 mM dithiothreitol, and 100 mM Bis-Tris, pH 5.5
SULT1D1 complexed with donor substrate 3''-phosphoadenosine 5''-phosphosulfate and accepter substrate p-nitrophenol, hanging drop vapor diffusion method, using 50 mM Tris-HCl (pH 7.9), 150 mM NaCl, 10 mM dithiothreitol, 16% (w/v) PEG 10000, 100 mM Bis-Tris (pH 5.5), 25% (v/v) glycerol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C66S
-
mutant is catalytically active, can not be activated by glutathione disulfide
F138A
-
25fold increase in KM-value for (R)-(-)-tetrahydro-1-naphthol. Unlike the wild-type enzyme the mutant enzyme is also active with (S)-(+)-1,2,3,4-tetrahydro-1-naphthol
F77A
-
83.3fold increase in KM-value for (R)-(-)-tetrahydro-1-naphthol,unlike the wild-type enzyme the mutant enzyme is also active with (S)-(+)-1,2,3,4-tetrahydro-1-naphthol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, stable for 6 months in sodium acetate buffer, pH 5.5, 0.25 M sucrose, 10% glycerol, 1 mM dithiothreitol at protein concentration of 1 mg/ml
-
4°C, 10 mM potassium phosphate, pH 6.8, 250 mM sucrose and 0.02% w/v NaN3, no more than 10% loss of activity after 5 months
-
4°C, sodium phosphate buffer, pH 7.0, 0.25 M sucrose, 5 mM 2-mercaptoethanol, 3 mM NaN3, 5% loss of activity per week at protein concentration between 0.5 and 1 mg/ml
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sekura, R.D.; Jakoby, W.B.
Aryl sulfotransferase IV from rat liver
Arch. Biochem. Biophys.
211
352-359
1981
Rattus norvegicus
brenda
Duffel, M.W.; Jakoby, W.B.
On the mechanism of aryl sulfotransferase
J. Biol. Chem.
256
11123-11127
1981
Rattus norvegicus
brenda
Mattock, P.; Jones, J.G.
Partial purification and properties of an enzyme from rat liver that catalyses the sulphation of L-tyrosyl derivatives
Biochem. J.
116
797-803
1970
Rattus norvegicus
brenda
Mattock, P.; Barford, D.J.; Basford, J.M.; Jones, J.G.
The effect of substrate concentration and pH on the enzymic sulphation of L-tyrosyl derivatives
Biochem. J.
116
805-810
1970
Rattus norvegicus
brenda
Zheng, Y.; Bergold, A.; Duffel, M.W.
Affinity labeling of aryl sulfotransferase IV. Identification of a peptide sequence at the binding site for 3-phosphoadenosine-5-phosphosulfate
J. Biol. Chem.
269
30313-30319
1994
Rattus norvegicus
brenda
Barford, D.J.; Jones, J.G.
The physiological role of L-tyrosine methyl sulphotransferase
Biochem. J.
125
76P-77P
1971
Rattus norvegicus
brenda
Vargas, F.; Frerot, O.; Tuong, M.D.T.; Schwartz, J.C.
Characterization of a tyrosine sulfotransferase in rat brain using cholecystokinin derivatives as acceptors
Biochemistry
24
5938-5943
1985
Rattus norvegicus
brenda
Saidha, T.; Schiff, J.A.
Purification and properties of a phenol sulphotransferase from Euglena using L-tyrosine as substrate
Biochem. J.
298
45-50
1994
Euglena gracilis
brenda
Sekura, R.D.; Duffel, M.W.; Jakoby, W.B.
Aryl sulfotransferases
Methods Enzymol.
77
197-206
1981
Rattus norvegicus
brenda
Guo, W.X.; Yang, Y.S.; Chen, X.; McPhie, P.; Jakoby, W.B.
Changes in substrate specificity of the recombinant form of phenol sulfotransferase IV (tyrosine-ester sulfotransferase)
Chem. Biol. Interact.
92
25-31
1994
Rattus norvegicus
brenda
Burkart, M.D.; Wong, C.H.
A continuous assay for the spectrophotometric analysis of sulfotransferases using aryl sulfotransferase IV
Anal. Biochem.
274
131-137
1999
Rattus norvegicus
brenda
Chapman, E.; Bryan, M.C.; Wong, C.H.
Mechanistic studies of beta-arylsulfotransferase IV
Proc. Natl. Acad. Sci. USA
100
910-915
2003
Rattus norvegicus
brenda
Chen, G.; Baron, J.; Duffel, M.W.
Enzyme- and sex-specific differences in the intralobular localizations and distributions of aryl sulfotransferase IV (tyrosine-ester sulfotransferase) and alcohol (hydroxysteroid) sulfotransferase a in rat liver
Drug Metab. Dispos.
23
1346-1353
1995
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Chen, X.; Yang, Y.S.; Zheng, Y.; Martin, B.M.; Duffel, M.W.; Jakoby, W.B.
Tyrosine-ester sulfotransferase from rat liver: Bacterial expression and identification
Protein Expr. Purif.
3
412-426
1992
Rattus norvegicus
-
brenda
Duffel, M.W.
Molecular specificity of aryl sulfotransferase IV (tyrosine-ester sulfotransferase) for xenobiotic substrates and inhibitors
Chem. Biol. Interact.
92
3-14
1994
Rattus norvegicus
brenda
King, R.S.; Duffel, M.W.
Oxidation-dependent inactivation of aryl sulfotransferase IV by primary N-hydroxy arylamines during in vitro assays
Carcinogenesis
18
843-849
1997
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
King, R.S.; Sharma, V.; Pedersen, L.C.; Kakuta, Y.; Negishi, M.; Duffel, M.W.
Structure-function modeling of the interactions of N-alkyl-N-hydroxyanilines with rat hepatic aryl sulfotransferase IV
Chem. Res. Toxicol.
13
1251-1258
2000
Rattus norvegicus
brenda
Malejka-Giganti, D.; Ringer, D.P.; Vijayaraghavan, P.; Kiehlbauch, C.C.; Kong, J.
Aryl sulfotransferase IV deficiency in rat liver carcinogenesis initiated with diethylnitrosamine and promoted with N-2-fluorenylacetamide or its C-9-oxidized metabolites
Exp. Mol. Pathol.
64
63-77
1997
Rattus norvegicus
brenda
Marshall, A.D.; Darbyshire, J.F.; McPhie, P.; Jakoby, W.B.
A review of the effects of manipulation of the cysteine residues of rat aryl sulfotransferase IV
Chem. Biol. Interact.
109
107-116
1998
Rattus norvegicus
brenda
Ringer, D.P.; Yerokun, T.; Khan, A.S.
Molecular mechanisms for the regulation of aryl sulfotransferase IV expression during 2-acetylaminofluorene-induced hepatocarcinogenesis in rat
Chem. Biol. Interact.
92
343-350
1994
Rattus norvegicus
brenda
Zhu, X.; Veronese, M.E.; Iocco, P.; McMannus, M.E.
cDNA cloning and expression of a new form of human aryl sulfotransferase
Int. J. Biochem. Cell Biol.
28
565-571
1996
Homo sapiens (P50226), Homo sapiens
brenda
Sheng, J.J.; Saxena, A.; Duffel, M.W.
Influence of phenylalanines 77 and 138 on the stereospecificity of aryl sulfotransferase IV
Drug Metab. Dispos.
32
559-565
2004
Rattus norvegicus
brenda
Maiti, S.; Dutta, S.M.; Baker, S.M.; Zhang, J.; Narasaraju, T.; Liu, L.; Chen, G.
In vivo and in vitro oxidative regulation of rat aryl sulfotransferase IV (AST IV)
J. Biochem. Mol. Toxicol.
19
109-118
2005
Rattus norvegicus
brenda
Chung, K.H.; Ringer, D.P.; Shin, K.O.
Influence of dietary zinc, copper and cadmium levels on rat liver aryl sulfotransferase IV activity
Nutr. Sci.
9
20-28
2006
Rattus norvegicus
-
brenda
Chung, K.H.; Ringer, D.P.; Shin, K.O.
Effects of copper, zinc and cadmium on the recovery pattern of aryl sulfotransferase IV activity in rats fed 2-acetylaminoflourene diet
Nutr. Sci.
9
29-34
2006
Rattus norvegicus
-
brenda
Teramoto, T.; Sakakibara, Y.; Liu, M.C.; Suiko, M.; Kimura, M.; Kakuta, Y.
Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase--mSULT1D1
Biochem. Biophys. Res. Commun.
379
76-80
2009
Mus musculus (Q3UZZ6)
brenda
Teramoto, T.; Sakakibara, Y.; Liu, M.C.; Suiko, M.; Kimura, M.; Kakuta, Y.
Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate
Biochem. Biophys. Res. Commun.
383
83-87
2009
Mus musculus (Q3UZZ6), Mus musculus
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.8.2.9)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
