Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 2.8.2.22

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.8.2.22

Enzymes and Genes:
aryl-sulfate sulfotransferase Inferred from experiment : astA ( Eubacterium sp. A-44 )

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: aryl-sulfate sulfotransferase

Enzyme Commission Synonyms: arylsulfate-phenol sulfotransferase, arylsulfotransferase, ASST, arylsulfate sulfotransferase, arylsulfate:phenol sulfotransferase, astA (gene name)

Standard Gibbs Free Energy (ΔrG in kcal/mol): 0.0 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme, characterized from bacteria that colonize the human and mouse intestine, catalyses the transfer of a sulfate group from a phenol sulfate ester to other phenolic compounds. Activity is enhanced by Mg2+ and Mn2+ [Kim86a]. Unlike EC 2.8.2.9, tyrosine-ester sulfotransferase and EC 2.8.2.1, aryl sulfotransferase, the enzyme does not act on 3'-phosphoadenylyl-sulfate or adenosine 3',5'-bisphosphate [Kim86a]. The level of sulfation of polyphenols depends on the positions of the hydroxyl groups [Koizumi90, Koizumi91, KonishiImamura94]. Hydroxy groups of tyrosine residues in peptides such as angiotensin can also act as acceptors. The reaction proceeds according to a ping pong bi bi mechanism [Lee95d].

Citations: [Kim07b]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.8.2.22 , ENZYME:EC:2.8.2.22 , IUBMB-ExplorEnz:EC:2.8.2.22

Credits:
Revised 14-May-2012 by Caspi R , SRI International


References

Kim07b: Kim B, Hyun YJ, Lee KS, Kobashi K, Kim DH (2007). "Cloning, expression and purification of arylsulfate sulfotransferase from Eubacterium A-44." Biol Pharm Bull 30(1);11-4. PMID: 17202651

Kim86a: Kim DH, Konishi L, Kobashi K (1986). "Purification, characterization and reaction mechanism of novel arylsulfotransferase obtained from an anaerobic bacterium of human intestine." Biochim Biophys Acta 872(1-2);33-41. PMID: 3460636

Koizumi90: Koizumi M, Shimizu M, Kobashi K (1990). "Enzymatic sulfation of quercetin by arylsulfotransferase from a human intestinal bacterium." Chem Pharm Bull (Tokyo) 38(3);794-6. PMID: 2347024

Koizumi91: Koizumi M, Akao T, Kadota S, Kikuchi T, Okuda T, Kobashi K (1991). "Enzymatic sulfation of polyphenols related to tannins by arylsulfotransferase." Chem Pharm Bull (Tokyo) 39(10);2638-43. PMID: 1806284

KonishiImamura94: Konishi-Imamura L, Sato M, Dohi K, Kadota S, Namba T, Kobashi K (1994). "Enzymatic sulfation of glycosides and their corresponding aglycones by arylsulfate sulfotransferase from a human intestinal bacterium." Biol Pharm Bull 17(8);1018-22. PMID: 7820100

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lee95d: Lee NS, Kim BT, Kim DH, Kobashi K (1995). "Purification and reaction mechanism of arylsulfate sulfotransferase from Haemophilus K-12, a mouse intestinal bacterium." J Biochem 118(4);796-801. PMID: 8576095


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Tue Nov 25, 2014, BIOCYC13A.