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Information on EC 2.8.2.6 - choline sulfotransferase
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2.8.2.6 choline sulfotransferaseSpecify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
choline sulphokinase, PAPS:choline sulfotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
choline sulphokinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + choline = adenosine 3',5'-bisphosphate + choline sulfate
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:choline sulfotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9047-23-8
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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'-phosphoadenylylsulfate + N,N,N-triethylaminoethanol
adenosine 3',5'-bisphosphate + N,N,N-triethylaminoethanol O-sulfate
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2% of the activity with choline
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-
?
3'-phosphoadenylylsulfate + N,N-dimethylaminoethanol
adenosine 3',5'-bisphosphate + N,N-dimethylaminoethanol O-sulfate
3'-phosphoadenylylsulfate + N,N-dimethylethylaminoethanol
adenosine 3',5'-bisphosphate + N,N-dimethylethylaminoethanol O-sulfate
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-
-
-
?
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
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-
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ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
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sulfate transfer appears to be irreversible in vitro
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ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
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-
-
ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
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choline-O-sulfate-biosynthesis, plants accumulate nontoxic compatible osmolytes as osmoprotectants in response to salinity or drought stress
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ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
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-
-
ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
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equilibrium of the choline sulfokinase reaction lies far toward the direction of choline-O-sulfate formation, only 0.1% conversion of choline-O-sulfate to 3'-phosphoadenylylsulfate can be detected
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ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
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-
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ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
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in presence of ATP and MgCl2
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ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
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-
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ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
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in presence of ATP and MgCl2
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ir
3'-phosphoadenylylsulfate + N,N-dimethylaminoethanol
adenosine 3',5'-bisphosphate + N,N-dimethylaminoethanol O-sulfate
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-
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-
?
3'-phosphoadenylylsulfate + N,N-dimethylaminoethanol
adenosine 3',5'-bisphosphate + N,N-dimethylaminoethanol O-sulfate
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35% of the activity with choline
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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'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
-
-
-
ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
-
choline-O-sulfate-biosynthesis, plants accumulate nontoxic compatible osmolytes as osmoprotectants in response to salinity or drought stress
-
ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
-
-
-
ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
-
-
-
ir
3'-phosphoadenylylsulfate + choline
adenosine 3',5'-bisphosphate + choline sulfate
-
-
-
ir
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Chlorocholine
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competitive dead-end inhibitor with respect to choline, uncompetitive with respect to PAPS
choline-O-phosphate
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dead-end inhibitor, competitive inhibition with choline, linear mixed type inhibitor with respect to PAPS
Tetramethylammonium
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competitive dead-end inhibitor with respect to choline, uncompetitive with respect to PAPS
Trimethylammonium
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competitive dead-end inhibitor with respect to choline, uncompetitive with respect to PAPS
vinyl trimethylammonium
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neurine, competitive dead-end inhibitor with respect to choline, uncompetitive with respect to PAPS
additional information
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iodoacetate is less effective as inhibitor, di-isopropylfluorophosphate is without action
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additional information
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3,3-dimethylbutanol does not inhibit, enzyme is not significantly inhibited by methyl, butyl, pentyl or hexyl sulfates nor by p-nitrophenol or carnitine, EDTA is not inhibitory, sodium chloride, bromide and iodide have no effect
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3'-phosphoadenosine 5'-phosphosulfate
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choline sulfate formation is increased 5fold by 1.0 mM
adenosine 5'-phosphosulfate
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choline sulfate formation is increased 2.8fold by 10 mM
NaCl
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activity is increased at least 4fold by salinization with 40% v/v artificial sea water
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
3'-phosphoadenylylsulfate
-
pH 7.8, 37°C, N,N-dimethylaminoethanol as substrate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5 - 14
3',5'-ADP
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pH 7.8, 37°C depending on the choline concentration
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6 - 9.9
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about 50% of activity maximum at pH 7.6, about 70% of activity maximum at pH 9.9
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TEMPERATURE OPTIMUM
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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 12
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stable at room temperature in the pH range 8.0-11.0, above pH 11.0 enzyme is rapidly inactivated, 80% inactivation at pH 12.0, below pH 8.0 stablity declines slowly with decreasing pH, maximum stability at pH 8,5-10.5
643827
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46
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no loss of activity during 10 min at pH 9.2, 30% loss at pH 7.3, 34% loss at pH 5.0
58.5
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complete loss of activity at pH 5.0, 85% activity retained at pH 9.2
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
age-inactivated enzyme can be restored to full activity by 10 min preincubation with 50 mM mercaptoethanol, prolonged incubation for 24 h results in irreversible denaturation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25% sucrose, loses only about 20% of its activity after 1 month
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-20°C, freezing and storing for 3 days results in complete loss of activity
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0°C, purified enzyme relatively stable when stored in presence of 25% sucrose
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2°C, more stable after (NH4)2SO4 or acetone fractionation, activity is reduced by 85% during 4 weeks
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Orsi, B.A.; Spencer, B.
Choline sulphokinase (sulfotransferase)
J. Biochem.
56
81-91
1964
Aspergillus nidulans
brenda
Fitzgerald, J.W.; Luschinski, P.C.
Further studies on the formation of choline sulfate by bacteria
Can. J. Microbiol.
23
483-490
1977
Pseudomonas sp., Pseudomonas sp. C12B
brenda
Renosto, F.; Segel, I.H.
Choline sulfokinase of Penicillium chrysogenum: partial purification and kinetic mechanism
Arch. Biochem. Biophys.
180
416-428
1977
Penicillium chrysogenum
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Rivoal, J.; Hanson, A.D.
Choline-O-sulfate biosynthesis in plants
Plant Physiol.
106
1187-1193
1994
Limonium perezii, Limonium latifolium, Limonium nashii, Limonium ramosissimum, Limonium sinuatum, no activity in Brassica napus, no activity in Brassica oleracea, no activity in Helianthus annuus, no activity in Hordeum vulgare, no activity in Zea mays
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