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Information on EC 2.8.2.10 - Renilla-luciferin sulfotransferase
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2.8.2.10 Renilla-luciferin sulfotransferaseIUBMB Comments
The product may be identical with Watasenia luciferin.
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Word Map
- 2.8.2.10
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acetobacter
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gdp-14cmannose
- glycosyltransferases
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xylinum
- polysaccharides
- cellobiose
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bioluminescence
The enzyme appears in viruses and cellular organisms
Synonyms
Lst, luciferin sulfokinase, luciferin sulfokinase(3'-phosphoadenylyl sulfate:luciferin sulfotransferase), luciferin sulfotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Lst
luciferin sulfokinase
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luciferin sulfokinase(3'-phosphoadenylyl sulfate:luciferin sulfotransferase)
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luciferin sulfotransferase
luciferin sulfotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + Renilla luciferin = adenosine 3',5'-bisphosphate + luciferyl sulfate
the product may be identical with Watasenia luciferin
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:Renilla luciferin sulfotransferase
The product may be identical with Watasenia luciferin.
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CAS REGISTRY NUMBER
COMMENTARY
37278-33-4
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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'-phosphoadenylyl sulfate + Cypridina luciferin
adenosine 3',5'-bisphosphate + Cypridina luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
adenosine 3',5'-bisphosphate + Cypridina luciferyl sulfate
3'-phosphoadenylyl sulfate + Cypridina luciferin
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r
benzyl luciferin + 3'-phosphoadenylylsulfate
benzyl luciferyl sulfate + adenosine 3',5'-bisphosphate
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fully active analog of coelenterate-type luciferin, equally effective as substrate
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r
benzyl luciferyl sulfate + adenosine 3',5'-bisphosphate
benzyl luciferin + 3'-phosphoadenylylsulfate
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r
Renilla luciferyl sulfate + adenosine 3',5'-bisphosphate
Renilla luciferin + 3'-phosphoadenylylsulfate
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
Renilla luciferyl sulfate + adenosine 3',5'-bisphosphate
Renilla luciferin + 3'-phosphoadenylylsulfate
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r
Renilla luciferyl sulfate + adenosine 3',5'-bisphosphate
Renilla luciferin + 3'-phosphoadenylylsulfate
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r
additional information
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enzyme is appparently specific for luciferin, does not exhibit any phenol sulfokinase activity
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additional information
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CoA can act as a sulfate acceptor in the sulfotransferase reaction, and can also competitively inhibit the sulfotransferase. Sulfotransferase(s) in Cypridina specimens can efficiently use CoA, 5'-AMP and 3'-AMP as a sulfate acceptor from Cypridina luciferyl sulfate and produce Cypridina luciferin, similar to the case with PAP. Mass spectral analyses of the sulfated products of 5'-AMP, 3'-AMP, and CoA
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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 + Cypridina luciferin
adenosine 3',5'-bisphosphate + Cypridina luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
adenosine 3',5'-bisphosphate + Cypridina luciferyl sulfate
3'-phosphoadenylyl sulfate + Cypridina luciferin
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r
Renilla luciferyl sulfate + adenosine 3',5'-bisphosphate
Renilla luciferin + 3'-phosphoadenylylsulfate
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
3'-phosphoadenylyl sulfate + Renilla luciferin
adenosine 3',5'-bisphosphate + luciferyl sulfate
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r
Renilla luciferyl sulfate + adenosine 3',5'-bisphosphate
Renilla luciferin + 3'-phosphoadenylylsulfate
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r
Renilla luciferyl sulfate + adenosine 3',5'-bisphosphate
Renilla luciferin + 3'-phosphoadenylylsulfate
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r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CoA
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CoA may be the competitive inhibitor against PAP in Cypridina sulfotransferase(s) and can also act as a sulfate acceptor
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Vargula hilgendorfii, collected at Chita (Aichi, Japan) on August 4, 2011, and Naruto (Tokushima, Japan) on August 24, 2017
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brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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in Cypridina (Vargula) hilgendorfii, Cypridina luciferin is converted from Cypridina luciferyl sulfate by a sulfotransferase with adenosine 3',5'-diphosphate (PAP), and is used for the luminescence reaction of Cypridina luciferase. The luminescence activity of crude extracts of Cypridina hilgendorfii is significantly stimulated by the addition of acetic acid. This stimulation may be explained by an efficient supply of PAP from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) catalyzed by the sulfotransferase. Acetic acid acts as a sulfate acceptor from PAPS, followed by forming acetyl sulfate and PAP. The structure of acetyl sulfate is identified using mass spectrometry and it spontaneously decomposed to acetic acid and free sulfate ion in aqueous solutions. This enzymatic conversion from Cypridina luciferyl sulfate to Cypridina luciferin coupled with acetic acid and PAPS by the luciferin sulfotransferase, enzymatic cycling of Cypridina luciferyl sulfate to Cypridina luciferin coupled with acetic acid and PAPS
physiological function
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in the luminous ostracod Cypridina (presently Vargula) hilgendorfii, Cypridina luciferyl sulfate (3-enol sulfate of Cypridina luciferin) is converted to Cypridina luciferin by a sulfotransferase with 3'-phosphoadenosine-5'-phosphate (PAP) as a sulfate acceptor. The resultant Cypridina luciferin is used for the luciferase-luciferin reaction of Cypridina to emit blue light. the addition of CoA to the crude extracts significantly stimulates luminescence intensity. CoA can act as a sulfate acceptor from Cypridina luciferyl sulfate. In addition, the sulfate group of Cypridina luciferyl sulfate is also transferred to adenosine 5'-monophosphate (5'-AMP) and adenosine 3'-monophosphate (3'-AMP) by the sulfotransferase. Other adenosine derivatives of 5'-AMP and 3'-AMP can also act as efficient sulfate acceptors on the millimolar order from Cypridina luciferyl sulfate by the sulfotransferase and they stimulate light emission in crude extracts of Cypridina specimens. ATP, NADH, and NAD+ weakly stimulate the luminescence activity
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is labile, can be stabilized by continous presence of 0.05 ml/l 2-mercaptoethanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, requirement of 2-mercaptoethanol in storage buffer, stable for at least several months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cormier, M.J.; Hori, K.; Karkhanis, Y.D.
Studies on the bioluminescence of Renilla reniformis. VII. Conversion of luciferin into luciferyl sulfate by luciferin sulfokinase
Biochemistry
9
1184-1189
1970
Renilla reniformis
brenda
Anderson, J.M.; Hori, K.; Cormier, M.J.
A bioluminescence assay for PAP(3',5'-diphosphoadenosine) and PAPS (3'-phosphoadenylyl sulfate)
Methods Enzymol.
57
244-257
1978
Renilla reniformis
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brenda
Fallon, T.R.; Li, F.S.; Vicent, M.A.; Weng, J.K.
Sulfoluciferin is biosynthesized by a specialized luciferin sulfotransferase in fireflies
Biochemistry
55
3341-3344
2016
Ellychnia corrusca, Ignelater luminosus, Photinus pyralis (A0A173GP47), Photinus pyralis, Photuris, Pyractomena
brenda
Nakamura, M.; Suzuki, T.; Ishizaka, N.; Sato, J.; Inouye, S.
Identification of 3-enol sulfate of Cypridina luciferin, Cypridina luciferyl sulfate, in the sea-firefly Cypridina (Vargula) hilgendorfii
Tetrahedron
70
2161-2168
2014
Vargula hilgendorfii
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brenda
Nakamura, M.; Matsuda, K.; Morikawa, T.; Ishizuka, K.; Inouye, S.
Efficient conversion to Cypridina luciferin from Cypridina luciferyl sulfate, coupled with enzymatic sulfation of acetic acid
Biochem. Biophys. Res. Commun.
529
678-684
2020
Vargula hilgendorfii
brenda
Nakamura, M.; Matsuda, K.; Nakamura, M.; Yamashita, K.; Suzuki, T.; Inouye, S.
Enzymatic conversion of Cypridina luciferyl sulfate to Cypridina luciferin with coenzyme A as a sulfate acceptor in Cypridina (Vargula) hilgendorfii
Photochem. Photobiol.
95
1376-1386
2019
Vargula hilgendorfii
brenda
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