Literature summary for 2.8.2.14 extracted from

Feng, L.; Yuen, Y.L.; Xu, J.; Liu, X.; Chan, M.Y.; Wang, K.; Fong, W.P.; Cheung, W.T.; Lee, S.S.
Identification and characterization of a novel PPARalpha-regulated and 7alpha-hydroxyl bile acid-preferring cytosolic sulfotransferase mL-STL (Sult2a8) (2017), J. Lipid Res., 58, 1114-1131 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene Sult2a8, DNA and amino acid sequence determination and analysis, mL-STL cDNAs exhibit multiple 5' termini and skipping of nucleotides, sequence analysis of 12 mL-STL 3'-RACE clones. The mL-STL gene has multiple alternative exonic splicing variants, long and short forms of mL-STL cDNAs. The long-form mL-STL gene is composed of seven exons separated by six introns, with a total gene size of 35902 bp. Recombinant expression of non-tagged and His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS, half of the expressed protein is soluble, whereas the remaining protein is misfolded to form inclusion bodies	Mus musculus

Cloned (Comment)

Organism

gene Sult2a8, DNA and amino acid sequence determination and analysis, mL-STL cDNAs exhibit multiple 5' termini and skipping of nucleotides, sequence analysis of 12 mL-STL 3'-RACE clones. The mL-STL gene has multiple alternative exonic splicing variants, long and short forms of mL-STL cDNAs. The long-form mL-STL gene is composed of seven exons separated by six introns, with a total gene size of 35902 bp. Recombinant expression of non-tagged and His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS, half of the expressed protein is soluble, whereas the remaining protein is misfolded to form inclusion bodies

Mus musculus

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	no significant substrate inhibition is detected in most compounds tested as the substrate concentrations increased from 0.01 to 0.1 mM	Mus musculus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Mus musculus	5829	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
3'-phosphoadenylyl sulfate + alpha-muricholic acid	Mus musculus	-	adenosine 3',5'-bisphosphate + alpha-muricholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + alpha-muricholic acid	Mus musculus SV/129	-	adenosine 3',5'-bisphosphate + alpha-muricholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + beta-muricholic acid	Mus musculus	low activity	adenosine 3',5'-bisphosphate + beta-muricholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + beta-muricholic acid	Mus musculus SV/129	low activity	adenosine 3',5'-bisphosphate + beta-muricholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + chenodeoxycholic acid	Mus musculus	-	adenosine 3',5'-bisphosphate + chenodeoxycholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + chenodeoxycholic acid	Mus musculus SV/129	-	adenosine 3',5'-bisphosphate + chenodeoxycholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + cholic acid	Mus musculus	-	adenosine 3',5'-bisphosphate + cholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + cholic acid	Mus musculus SV/129	-	adenosine 3',5'-bisphosphate + cholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + glycochenodeoxycholic acid	Mus musculus	-	adenosine 3',5'-bisphosphate + glycochenodeoxycholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + glycocholic acid	Mus musculus	-	adenosine 3',5'-bisphosphate + glycocholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + taurochenodeoxycholic acid	Mus musculus	-	adenosine 3',5'-bisphosphate + taurochenodeoxycholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + taurocholic acid	Mus musculus	-	adenosine 3',5'-bisphosphate + taurocholate 3-sulfate	-	?

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q8BGL3	-	-
Mus musculus SV/129	Q8BGL3	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration, to homogeneity	Mus musculus

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	liver mRNA expression profiles between wild-type mice under fed or 72 h fasted states using the mRNA FDD analysis and isolated a 910 bp partial cDNA fragment	Mus musculus	-
additional information	no detectable expression of mL-STL mRNA is found in other mouse tissues, including the stomach, small intestine, cecum, colon, kidney, heart, lung, spleen, brain, brown fat, white fat, smooth muscle, testis, and ovaries	Mus musculus	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
155.85	-	pH 5.5, 37°C, purified recombinant wild-type enzyme, substrate beta-muricholic acid	Mus musculus
274.1	-	pH 5.5, 37°C, purified recombinant wild-type enzyme, substrate ursodeoxycholic acid	Mus musculus
485.1	720.7	pH 5.5, 37°C, purified recombinant wild-type enzyme, substrate taurocholic acid	Mus musculus
579	652.3	pH 5.5, 37°C, purified recombinant wild-type enzyme, substrate cholic acid	Mus musculus
649.9	960.1	pH 5.5, 37°C, purified recombinant wild-type enzyme, substrate glycocholic acid	Mus musculus
854.4	-	pH 5.5, 37°C, purified recombinant wild-type enzyme, substrate alpha-muricholic acid	Mus musculus
1154.3	1287.4	pH 5.5, 37°C, purified recombinant wild-type enzyme, substrate chenodeoxycholic acid	Mus musculus
1294.7	-	pH 5.5, 37°C, purified recombinant wild-type enzyme, substrate taurochenodeoxycholic acid	Mus musculus
1380.2	-	pH 5.5, 37°C, purified recombinant wild-type enzyme, substrate glycochenodeoxycholic acid	Mus musculus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
3'-phosphoadenylyl sulfate + alpha-muricholic acid	-	Mus musculus	adenosine 3',5'-bisphosphate + alpha-muricholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + alpha-muricholic acid	-	Mus musculus SV/129	adenosine 3',5'-bisphosphate + alpha-muricholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + beta-muricholic acid	low activity	Mus musculus	adenosine 3',5'-bisphosphate + beta-muricholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + beta-muricholic acid	low activity	Mus musculus SV/129	adenosine 3',5'-bisphosphate + beta-muricholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + chenodeoxycholic acid	-	Mus musculus	adenosine 3',5'-bisphosphate + chenodeoxycholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + chenodeoxycholic acid	-	Mus musculus SV/129	adenosine 3',5'-bisphosphate + chenodeoxycholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + cholic acid	-	Mus musculus	adenosine 3',5'-bisphosphate + cholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + cholic acid	-	Mus musculus SV/129	adenosine 3',5'-bisphosphate + cholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + glycochenodeoxycholic acid	-	Mus musculus	adenosine 3',5'-bisphosphate + glycochenodeoxycholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + glycocholic acid	-	Mus musculus	adenosine 3',5'-bisphosphate + glycocholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + taurochenodeoxycholic acid	-	Mus musculus	adenosine 3',5'-bisphosphate + taurochenodeoxycholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + taurocholic acid	-	Mus musculus	adenosine 3',5'-bisphosphate + taurocholate 3-sulfate	-	?
3'-phosphoadenylyl sulfate + ursodeoxycholic acid	low activity	Mus musculus	adenosine 3',5'-bisphosphate + ursodeoxycholate 3-sulfate	-	?
additional information	recombinant His-tagged mL-STL protein preferentially catalyzes primary bile acid substrates. Low mL-STL-mediated SULT activity is observed with beta-muricholic acid (beta-MCA), and ursodeoxycholic acid (UDCA), whereas very low activity is observed in omega-muricholic (omega-MCA), deoxycholic acid, lithocholic acid, taurolithocholic acid sodium salt, androsterone, dehydroepiandrosterone (DHEA), pregnenolone, cholesterol, 22(S)-hydroxycholesterol, 22(R)-hydroxycholesterol, and corticosterone, substrate specificity, overview. His-tagged mL-STL protein displays relatively low substrate specificity toward the SULT1 prototype substrates examined	Mus musculus	?	-	-
additional information	recombinant His-tagged mL-STL protein preferentially catalyzes primary bile acid substrates. Low mL-STL-mediated SULT activity is observed with beta-muricholic acid (beta-MCA), and ursodeoxycholic acid (UDCA), whereas very low activity is observed in omega-muricholic (omega-MCA), deoxycholic acid, lithocholic acid, taurolithocholic acid sodium salt, androsterone, dehydroepiandrosterone (DHEA), pregnenolone, cholesterol, 22(S)-hydroxycholesterol, 22(R)-hydroxycholesterol, and corticosterone, substrate specificity, overview. His-tagged mL-STL protein displays relatively low substrate specificity toward the SULT1 prototype substrates examined	Mus musculus SV/129	?	-	-

Synonyms

Synonyms	Comment	Organism
mL-STL	-	Mus musculus
More	cf. EC 2.8.2.1	Mus musculus
mouse liver-sulfotransferase-like	-	Mus musculus
sulfotransferase	-	Mus musculus
SULT2A8	-	Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Mus musculus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.5	-	recombinant enzyme	Mus musculus

Expression

Organism	Comment	Expression
Mus musculus	Wy-14,643 treatment downregulates mL-STL expression in a time- and PPARalpha-dependent manner. Two weeks of Wy-14,643 treatment result in dramatic suppression of mLSTL mRNA and protein expressions in the wild-type, but not in KO, mice, suggesting that the downregulation is mediated through the activation of PPARalpha upon Wy-14,643 treatment	down
Mus musculus	liver mRNA expression profiles between wild-type mice and PPARalpha-null mice under fed or 72 h fasted states using the mRNA FDD analysis and isolated a 910 bp partial cDNA fragment. Fasting has a time-dependent inhibition on the mL-STL protein expression in the KO mice, but not significantly in the wild-type mice	additional information
Mus musculus	PPARalpha is required to sustain Sult2a8 expression during fasting	up

General Information

General Information	Comment	Organism
evolution	full-length mL-STL cDNA has alternative exonic splicing variants and shares high amino acid sequence homology to the SULT2A family. The mL-STL gene belongs to the Sult2a family of a superfamily of cytosolic SULTs	Mus musculus
physiological function	SULT2A8/mL-STL is a PPARalpha-regulated and 7alpha-hydroxylated bile acid-preferring cytosolic sulfotransferase, it is a liver-specific and male-dominant protein. PPARalpha modulates the homeostasis of bile acids during fasting being an essential regulator in bile acid biotransformation via sulfonation during fasting. The enzyme reveals a narrow sulfonating activity toward 7alpha-hydroxyl primary bile acids, including cholic acid, chenodeoxycholic acid, and alpha-muricholic acid, and thus may be the major hepatic bile acid sulfonating enzyme in mice	Mus musculus