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Literature summary for 2.8.2.32 extracted from

  • Kurogi, K.; Yoshihama, M.; Horton, A.; Schiefer, I.; Krasowski, M.; Hagey, L.; Williams, F.; Sakakibara, Y.; Kenmochi, N.; Suiko, M.; Liu, M.
    Identification and characterization of 5alpha-cyprinol-sulfating cytosolic sulfotransferases (Sults) in the zebrafish (Danio rerio) (2017), J. Steroid Biochem. Mol. Biol., 174, 120-127 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
5alpha-cyprinol substrate inhibition; substrate inhibition; substrate inhibition kinetics Danio rerio
5alpha-cyprinol substrate inhibition kinetics Homo sapiens
5beta-cyprinol substrate inhibition; substrate inhibition Danio rerio
additional information the sulfation of both of 5alpha-cyprinol and 5beta-cyprinol by zebrafish Sult2st2 and Sult2st3 can be fitted to substrate inhibition kinetics; the sulfation of both of 5alpha-cyprinol and 5beta-cyprinol by zebrafish Sult2st2 and Sult2st3 can be fitted to substrate inhibition kinetics Danio rerio

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics, kinetic analysis Danio rerio
additional information
-
additional information Michaelis-Menten kinetics for beta-cyprinol, kinetic analysis Homo sapiens
additional information
-
additional information Michaelis-Menten kinetics for beta-cyprinol, kinetic analysis Danio rerio

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-
cytosol
-
Danio rerio 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3'-phosphoadenylyl sulfate + 5alpha-cyprinol Homo sapiens
-
adenosine 3',5'-bisphosphate + 5alpha-cyprinol sulfate
-
?
3'-phosphoadenylyl sulfate + 5alpha-cyprinol Danio rerio
-
adenosine 3',5'-bisphosphate + 5alpha-cyprinol sulfate
-
?
3'-phosphoadenylyl sulfate + 5beta-cyprinol Homo sapiens
-
adenosine 3',5'-bisphosphate + 5beta-cyprinol sulfate
-
?
3'-phosphoadenylyl sulfate + 5beta-cyprinol Danio rerio
-
adenosine 3',5'-bisphosphate + 5beta-cyprinol sulfate
-
?

Organism

Organism UniProt Comment Textmining
Danio rerio A0A0R4IT32
-
-
Danio rerio A4FUP0
-
-
Danio rerio Q1L874
-
-
Homo sapiens Q06520
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00034
-
substrate 5beta-cyprinol, pH 7.0, 37°C, purified recombinant enzyme Homo sapiens
0.00115
-
substrate 5beta-cyprinol, pH 7.0, 28°C, purified recombinant enzyme Danio rerio
0.00143
-
substrate 5alpha-cyprinol, pH 7.0, 28°C, purified recombinant enzyme Danio rerio
0.00471
-
substrate 5alpha-cyprinol, pH 7.0, 37°C, purified recombinant enzyme Homo sapiens
0.01008
-
substrate 5beta-cyprinol, pH 7.0, 28°C, purified recombinant enzyme Danio rerio
0.01014
-
substrate 5alpha-cyprinol, pH 7.0, 28°C, purified recombinant enzyme Danio rerio
0.02642
-
substrate 5beta-cyprinol, pH 7.0, 28°C, purified recombinant enzyme Danio rerio
0.02768
-
substrate 5alpha-cyprinol, pH 7.0, 28°C, purified recombinant enzyme Danio rerio

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3'-phosphoadenylyl sulfate + 5alpha-cyprinol
-
Homo sapiens adenosine 3',5'-bisphosphate + 5alpha-cyprinol sulfate
-
?
3'-phosphoadenylyl sulfate + 5alpha-cyprinol
-
Danio rerio adenosine 3',5'-bisphosphate + 5alpha-cyprinol sulfate
-
?
3'-phosphoadenylyl sulfate + 5alpha-cyprinol 3alpha,7alpha,12alpha,26,27-pentahydroxy-5alpha-cholestane Homo sapiens adenosine 3',5'-bisphosphate + 5alpha-cyprinol sulfate
-
?
3'-phosphoadenylyl sulfate + 5alpha-cyprinol 3alpha,7alpha,12alpha,26,27-pentahydroxy-5alpha-cholestane Danio rerio adenosine 3',5'-bisphosphate + 5alpha-cyprinol sulfate
-
?
3'-phosphoadenylyl sulfate + 5beta-cyprinol
-
Homo sapiens adenosine 3',5'-bisphosphate + 5beta-cyprinol sulfate
-
?
3'-phosphoadenylyl sulfate + 5beta-cyprinol
-
Danio rerio adenosine 3',5'-bisphosphate + 5beta-cyprinol sulfate
-
?
additional information NMR and mass spectrometry analysis of the reaction products. Human SULT2A1 shows substrate inhibition kinetics for 5alpha-cyprinol and Michaelis-Menten kinetics for beta-cyprinol. High activity with dehydroepiandrosterone (DHEA), cf. EC 2.8.2.2 Homo sapiens ?
-
-
additional information NMR and mass spectrometry analysis of the reaction products. The sulfation of both of 5alpha-cyprinol and 5beta-cyprinol by zebrafish Sult2st2 and Sult2st3 can be fitted to substrate inhibition kinetics. No activity with 3alpha,7alpha,12alpha-trihydroxy-5alpha-cholestanoic acid (5alpha-TriOH CA), dehydroepiandrosterone (DHEA) is a poor substrate Danio rerio ?
-
-
additional information NMR and mass spectrometry analysis of the reaction products. Zebrafish Sult3st4 shows substrate inhibition kinetics for 5alpha-cyprinol and Michaelis-Menten kinetics for beta-cyprinol. High activity with dehydroepiandrosterone (DHEA), cf. EC 2.8.2.2 Danio rerio ?
-
-

Synonyms

Synonyms Comment Organism
5alpha-cyprinol-sulfating cytosolic sulfotransferase
-
Homo sapiens
5alpha-cyprinol-sulfating cytosolic sulfotransferase
-
Danio rerio
5alpha-cyprinol-sulfating Sult
-
Homo sapiens
5alpha-cyprinol-sulfating Sult
-
Danio rerio
More cf. EC 2.8.2.2 Homo sapiens
SULT2A1
-
Homo sapiens
sult2st2
-
Danio rerio
sult2st3
-
Danio rerio
Sult3st4
-
Danio rerio

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
28
-
assay at Danio rerio
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Danio rerio
7.5 9.5 broad optimum Homo sapiens
8.5
-
-
Danio rerio
9.5
-
-
Danio rerio

pH Range

pH Minimum pH Maximum Comment Organism
6 10.5 activity range of Sult2st3 Danio rerio
6 10.5 activity range, high activity within this range Danio rerio

General Information

General Information Comment Organism
evolution both Sult2st2 and Sult2st3 have evolved to sulfate specifically C27-bile alcohol, 5alpha-cyprinol, in Cypriniform fish, whereas the enzymatic characteristics of zebrafish Sult3 members, particularly Sult3st4, correlate with those of human SULT2A1. Whereas zebrafish Sult2 family members are active in the sulfation of bile alcohols, Sult3 family members sulfate 3beta-hydroxysteroids such as pregnenolone and DHEA Danio rerio
evolution both Sult2st2 and Sult2st3 have evolved to sulfate specifically C27-bile alcohol, 5alpha-cyprinol, in Cypriniform fish, whereas the enzymatic characteristics of zebrafish Sult3 members, particularly Sult3st4, correlate with those of human SULT2A1. Whereas zebrafish Sult2 family members are active in the sulfation of bile alcohols, Sult3 family members sulfate 3beta-hydroxysteroids such as pregnenolone and DHEA. Substrate recognition sites of zebrafish Sult2 and Sult3 family members differ significantly from those of human SULT2A1 Homo sapiens
evolution both Sult2st2 and Sult2st3 have evolved to sulfate specifically C27-bile alcohol, 5alpha-cyprinol, in Cypriniform fish, whereas the enzymatic characteristics of zebrafish Sult3 members, particularly Sult3st4, correlate with those of human SULT2A1. Whereas zebrafish Sult2 family members are active in the sulfation of bile alcohols, Sult3 family members sulfate 3beta-hydroxysteroids such as pregnenolone and DHEA. Substrate recognition sites of zebrafish Sult2 and Sult3 family members differ significantly from those of human SULT2A1 Danio rerio
physiological function Sult2st2 and Sult2st3 are the major 5alpha-cyprinol-sulfating Sults in zebrafish that sulfate 5alpha-cyprinol at C27 position. Both Sult2st2 and Sult2st3 apparently do not distinguish between 5alpha-cyprinol and 5beta-cyprinol, two bile salts with opposite A/B ring junctions Homo sapiens
physiological function Sult2st2 and Sult2st3 are the major 5alpha-cyprinol-sulfating Sults in zebrafish that sulfate 5alpha-cyprinol at C27 position. Both Sult2st2 and Sult2st3 apparently do not distinguish between 5alpha-cyprinol and 5beta-cyprinol, two bile salts with opposite A/B ring junctions Danio rerio