Sulfation: Difference between revisions
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tried to make the article clearer by improving its structure -- if this edit is wrong, then imo this article should either be deleted or renamed "tyrosine sulfation" |
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{{confusing|date=April 2021|reason=the article uses a lot of jargon (e.g. 'conjugation' -- why not just say e.g. 'bonding'? and the provided link for 'conjugation' does not actually provide a clear definition of the term) in the introduction, and does not clearly distinguish between a chemical pathway, the definition of a class of pathways that would be characterized by a common 'beginning' and 'final' molecule( type)s, particular/specific enzymes that are used to accomplish this pathway or some examples of this class of pathways in various organisms, or the specific mechanisms by which specific enzymes do the above. Compare e.g. there being different articles for the TCA cycle in particular, cellular respiration in general, ADP/ATP translocase, and ATP. It is unclear which analogous level of abstraction is meant to apply to the term 'sulfation'}} |
{{confusing|date=April 2021|reason=the article uses a lot of jargon (e.g. 'conjugation' -- why not just say e.g. 'bonding'? and the provided link for 'conjugation' does not actually provide a clear definition of the term) in the introduction, and does not clearly distinguish between a chemical pathway, the definition of a class of pathways that would be characterized by a common 'beginning' and 'final' molecule( type)s, particular/specific enzymes that are used to accomplish this pathway or some examples of this class of pathways in various organisms, or the specific mechanisms by which specific enzymes do the above. Compare e.g. there being different articles for the TCA cycle in particular, cellular respiration in general, ADP/ATP translocase, and ATP. It is unclear which analogous level of abstraction is meant to apply to the term 'sulfation'}} |
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'''Sulfation''' or '''sulfurylation''' in biochemistry is the [[enzyme]]-catalyzed [[Conjugation (biochemistry)|conjugation]] of a [[Sulfonic acid|sulfo group]] (not a [[sulfate]] or [[sulfuryl]] group) to another molecule.<ref name=":0">{{Cite journal|title = Sulfotransferases: Structure, Mechanism, Biological Activity, Inhibition, and Synthetic Utility|journal = Angewandte Chemie International Edition|date = 2004-07-05|issn = 1521-3773|pages = 3526–3548|volume = 43|issue = 27|doi = 10.1002/anie.200300631|first = Eli|last = Chapman|first2 = Michael D.|last2 = Best|first3 = Sarah R.|last3 = Hanson|first4 = Chi-Huey|last4 = Wong|pmid=15293241}}</ref> This biotransformation involves a [[sulfotransferase]] enzyme catalyzing the transfer of a sulfo group from a donor cosubstrate, usually [[3'-phosphoadenosine-5'-phosphosulfate]] (PAPS), to a substrate molecule's hydroxyl or amine, resulting in a [[sulfate]] or [[sulfamate]], respectively. Sulfation is involved in a variety of biological processes, including detoxification, hormone regulation, molecular recognition, cell signaling, and viral entry into cells.<ref name=":0" /> It is among the reactions in [[Drug metabolism#Phase II|phase II drug metabolism]], frequently effective in rendering a [[xenobiotic]] less active from a [[pharmacology|pharmacological]] and [[toxicology|toxicological]] standpoint, but sometimes playing a role in the activation of xenobiotics (e.g. [[aromatic amine]]s, methyl-substituted [[polycyclic aromatic hydrocarbon]]s). Another example of biological sulfation is in the synthesis of sulfonated [[glycosaminoglycan]]s, such as [[heparin]], [[heparan sulfate]], [[chondroitin sulfate]], and [[dermatan sulfate]]. Sulfation is also a possible [[posttranslational modification]] of proteins. |
'''Sulfation''' or '''sulfurylation''' in biochemistry is the [[enzyme]]-catalyzed [[Conjugation (biochemistry)|conjugation]] of a [[Sulfonic acid|sulfo group]] (not a [[sulfate]] or [[sulfuryl]] group) to another molecule.<ref name=":0">{{Cite journal|title = Sulfotransferases: Structure, Mechanism, Biological Activity, Inhibition, and Synthetic Utility|journal = Angewandte Chemie International Edition|date = 2004-07-05|issn = 1521-3773|pages = 3526–3548|volume = 43|issue = 27|doi = 10.1002/anie.200300631|first = Eli|last = Chapman|first2 = Michael D.|last2 = Best|first3 = Sarah R.|last3 = Hanson|first4 = Chi-Huey|last4 = Wong|pmid=15293241}}</ref> This biotransformation involves a [[sulfotransferase]] enzyme catalyzing the transfer of a sulfo group from a donor cosubstrate, usually [[3'-phosphoadenosine-5'-phosphosulfate]] (PAPS), to a substrate molecule's hydroxyl or amine, resulting in a [[sulfate]] or [[sulfamate]], respectively. Sulfation is involved in a variety of biological processes, including detoxification, hormone regulation, molecular recognition, cell signaling, and viral entry into cells.<ref name=":0" /> It is among the reactions in [[Drug metabolism#Phase II|phase II drug metabolism]], frequently effective in rendering a [[xenobiotic]] less active from a [[pharmacology|pharmacological]] and [[toxicology|toxicological]] standpoint, but sometimes playing a role in the activation of xenobiotics (e.g. [[aromatic amine]]s, methyl-substituted [[polycyclic aromatic hydrocarbon]]s). Another example of biological sulfation is in the synthesis of sulfonated [[glycosaminoglycan]]s, such as [[heparin]], [[heparan sulfate]], [[chondroitin sulfate]], and [[dermatan sulfate]]. Sulfation is also a possible [[posttranslational modification]] of proteins. |
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=Examples= |
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Sulfation occurs as a part of several important biological processes. |
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==Tyrosine sulfation== |
==Tyrosine sulfation== |
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Tyrosine sulfation is a [[posttranslational modification]] in which a [[tyrosine]] residue of a protein is sulfated by a [[tyrosylprotein sulfotransferase]] (TPST) typically in the [[Golgi apparatus]]. Secreted proteins and extracellular parts of membrane proteins that pass through the Golgi apparatus may be sulfated. Such sulfation was first discovered by [[Frederick Bettelheim|Bettelheim]] in bovine fibrinopeptide B in 1954<ref>{{cite journal | last1 = Bettelheim | first1 = F. R. | year = 1954 | title = Tyrosine-''O''-sulfate in a peptide from fibrinogen | journal = J. Am. Chem. Soc. | volume = 76 | issue = 10| pages = 2838–2839 | doi = 10.1021/ja01639a073 }}</ref> and later found be present in animals and plants but not in [[prokaryote]]s or in yeasts. Sulfation sites are tyrosine residues exposed on the surface of the protein typically surrounded by acidic residues. A detailed description of the characteristics of the sulfation site is available from PROSITE (PROSITE pattern: PS00003)[http://www.expasy.org/cgi-bin/nicedoc.pl?PS00003]. Two types of tyrosylprotein sulfotransferases (TPST-1 and TPST-2) have been identified. Recently identified RaxX protein from most Xanthomonas species contains tyrosine sulfation residue, and mimics the plant peptide hormone PSY (Amano et al., 2007, Pruitt et al., 2015, 2017). |
Tyrosine sulfation is a [[posttranslational modification]] in which a [[tyrosine]] residue of a protein is sulfated by a [[tyrosylprotein sulfotransferase]] (TPST) typically in the [[Golgi apparatus]]. Secreted proteins and extracellular parts of membrane proteins that pass through the Golgi apparatus may be sulfated. Such sulfation was first discovered by [[Frederick Bettelheim|Bettelheim]] in bovine fibrinopeptide B in 1954<ref>{{cite journal | last1 = Bettelheim | first1 = F. R. | year = 1954 | title = Tyrosine-''O''-sulfate in a peptide from fibrinogen | journal = J. Am. Chem. Soc. | volume = 76 | issue = 10| pages = 2838–2839 | doi = 10.1021/ja01639a073 }}</ref> and later found be present in animals and plants but not in [[prokaryote]]s or in yeasts. Sulfation sites are tyrosine residues exposed on the surface of the protein typically surrounded by acidic residues. A detailed description of the characteristics of the sulfation site is available from PROSITE (PROSITE pattern: PS00003)[http://www.expasy.org/cgi-bin/nicedoc.pl?PS00003]. Two types of tyrosylprotein sulfotransferases (TPST-1 and TPST-2) have been identified. Recently identified RaxX protein from most Xanthomonas species contains tyrosine sulfation residue, and mimics the plant peptide hormone PSY (Amano et al., 2007, Pruitt et al., 2015, 2017). |
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===Function=== |
===Function of tyrosine sulfation=== |
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Sulfation plays role in strengthening protein–protein interactions. Types of human proteins known to undergo tyrosine sulfation include adhesion molecules, G-protein-coupled receptors, coagulation factors, [[serine protease inhibitor]]s, extracellular matrix proteins, and hormones. Tyrosine ''O''-sulfate is a stable molecule and is excreted in urine in animals. No enzymatic mechanism of tyrosine sulfate desulfation is known to exist. |
Sulfation plays role in strengthening protein–protein interactions. Types of human proteins known to undergo tyrosine sulfation include adhesion molecules, G-protein-coupled receptors, coagulation factors, [[serine protease inhibitor]]s, extracellular matrix proteins, and hormones. Tyrosine ''O''-sulfate is a stable molecule and is excreted in urine in animals. No enzymatic mechanism of tyrosine sulfate desulfation is known to exist. |
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By knock-out of ''TPST'' genes in mice, it may be observed that tyrosine sulfation has effects on the growth of the mice, such as body weight, fecundity, and postnatal viability. |
By knock-out of ''TPST'' genes in mice, it may be observed that tyrosine sulfation has effects on the growth of the mice, such as body weight, fecundity, and postnatal viability. |
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===Regulation=== |
===Regulation of tyrosine sulfation=== |
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There is very limited evidence that the TPST genes are subject to transcriptional regulation and tyrosine ''O''-sulfate is very stable and cannot be easily degraded by mammalian sulfatases. Tyrosine ''O''-sulfation is an irreversible process ''in vivo''. An antibody called PSG2 shows high sensitivity and specificity for epitopes containing sulfotyrosine independent of the sequence context. New tools are being developed to study TPST's, using synthetic peptides and small molecule screens.<ref>{{cite journal | last1 = Byrne | first1 = D. P. | year = 2018 | title = New tools for evaluating protein tyrosine sulfation: tyrosylprotein sulfotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors | url = http://www.biochemj.org/content/475/15/2435.abstract| journal = Biochemical Journal | volume = 475 | issue = 15| pages = 2435–2455 | doi = 10.1042/BCJ20180266 | doi-access = free }}</ref> |
There is very limited evidence that the TPST genes are subject to transcriptional regulation and tyrosine ''O''-sulfate is very stable and cannot be easily degraded by mammalian sulfatases. Tyrosine ''O''-sulfation is an irreversible process ''in vivo''. An antibody called PSG2 shows high sensitivity and specificity for epitopes containing sulfotyrosine independent of the sequence context. New tools are being developed to study TPST's, using synthetic peptides and small molecule screens.<ref>{{cite journal | last1 = Byrne | first1 = D. P. | year = 2018 | title = New tools for evaluating protein tyrosine sulfation: tyrosylprotein sulfotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors | url = http://www.biochemj.org/content/475/15/2435.abstract| journal = Biochemical Journal | volume = 475 | issue = 15| pages = 2435–2455 | doi = 10.1042/BCJ20180266 | doi-access = free }}</ref> |
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==Seagrasses== |
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The evolution of several sulfotransferases appears to have facilitated the adaptation of the terrestrial ancestors of seagrasses to a new marine habitat.<ref name=Olsen2016 /><ref name=Pfeifer2020 /> |
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=See also= |
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*[[Glucuronidation]] |
*[[Glucuronidation]] |
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*[[Methylation]] |
*[[Methylation]] |
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*[[Acetylation]] |
*[[Acetylation]] |
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=References= |
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{{reflist |
{{reflist| refs= |
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<ref name=Olsen2016>{{cite journal |doi = 10.1038/nature16548|title = The genome of the seagrass Zostera marina reveals angiosperm adaptation to the sea|year = 2016|last1 = Olsen|first1 = Jeanine L.|last2 = Rouzé|first2 = Pierre|last3 = Verhelst|first3 = Bram|last4 = Lin|first4 = Yao-Cheng|last5 = Bayer|first5 = Till|last6 = Collen|first6 = Jonas|last7 = Dattolo|first7 = Emanuela|last8 = De Paoli|first8 = Emanuele|last9 = Dittami|first9 = Simon|last10 = Maumus|first10 = Florian|last11 = Michel|first11 = Gurvan|last12 = Kersting|first12 = Anna|last13 = Lauritano|first13 = Chiara|last14 = Lohaus|first14 = Rolf|last15 = Töpel|first15 = Mats|last16 = Tonon|first16 = Thierry|last17 = Vanneste|first17 = Kevin|last18 = Amirebrahimi|first18 = Mojgan|last19 = Brakel|first19 = Janina|last20 = Boström|first20 = Christoffer|last21 = Chovatia|first21 = Mansi|last22 = Grimwood|first22 = Jane|last23 = Jenkins|first23 = Jerry W.|last24 = Jueterbock|first24 = Alexander|last25 = Mraz|first25 = Amy|last26 = Stam|first26 = Wytze T.|last27 = Tice|first27 = Hope|last28 = Bornberg-Bauer|first28 = Erich|last29 = Green|first29 = Pamela J.|last30 = Pearson|first30 = Gareth A.|journal = Nature|volume = 530|issue = 7590|pages = 331–335|pmid = 26814964|bibcode = 2016Natur.530..331O|s2cid = 3713147|display-authors = 1}}</ref> |
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<ref name=Pfeifer2020>{{cite journal |doi = 10.3389/fpls.2020.588754|title = The Cell Wall of Seagrasses: Fascinating, Peculiar and a Blank Canvas for Future Research|year = 2020|last1 = Pfeifer|first1 = Lukas|last2 = Classen|first2 = Birgit|journal = Frontiers in Plant Science|volume = 11|page = 588754|pmid = 33193541|pmc = 7644952}} </ref> |
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}} |
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* {{cite journal |author=Moore KL |title=The biology and enzymology of protein tyrosine O-sulfation |journal=J. Biol. Chem. |volume=278 |issue=27 |pages=24243–6 |year=2003 |pmid=12730193 |doi= 10.1074/jbc.R300008200|url=http://www.jbc.org/cgi/content/full/278/27/24243|doi-access=free }} |
* {{cite journal |author=Moore KL |title=The biology and enzymology of protein tyrosine O-sulfation |journal=J. Biol. Chem. |volume=278 |issue=27 |pages=24243–6 |year=2003 |pmid=12730193 |doi= 10.1074/jbc.R300008200|url=http://www.jbc.org/cgi/content/full/278/27/24243|doi-access=free }} |
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* {{cite journal |author=Hoffhines AJ |title=Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody. |journal=J. Biol. Chem. |volume=281 |issue=49 |pages=37877–87 |year=2006 |pmid=17046811 |doi=10.1074/jbc.M609398200 |last2=Damoc |first2=E |last3=Bridges |first3=KG |last4=Leary |first4=JA |last5=Moore |first5=KL |pmc=1764208}} |
* {{cite journal |author=Hoffhines AJ |title=Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody. |journal=J. Biol. Chem. |volume=281 |issue=49 |pages=37877–87 |year=2006 |pmid=17046811 |doi=10.1074/jbc.M609398200 |last2=Damoc |first2=E |last3=Bridges |first3=KG |last4=Leary |first4=JA |last5=Moore |first5=KL |pmc=1764208}} |
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{{Protein primary structure}} |
{{Protein primary structure}} |
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Revision as of 16:57, 3 April 2021
 | This article may be confusing or unclear to readers. In particular, the article uses a lot of jargon (e.g. 'conjugation' -- why not just say e.g. 'bonding'? and the provided link for 'conjugation' does not actually provide a clear definition of the term) in the introduction, and does not clearly distinguish between a chemical pathway, the definition of a class of pathways that would be characterized by a common 'beginning' and 'final' molecule( type)s, particular/specific enzymes that are used to accomplish this pathway or some examples of this class of pathways in various organisms, or the specific mechanisms by which specific enzymes do the above. Compare e.g. there being different articles for the TCA cycle in particular, cellular respiration in general, ADP/ATP translocase, and ATP. It is unclear which analogous level of abstraction is meant to apply to the term 'sulfation'. (April 2021) |
Sulfation or sulfurylation in biochemistry is the enzyme-catalyzed conjugation of a sulfo group (not a sulfate or sulfuryl group) to another molecule.[1] This biotransformation involves a sulfotransferase enzyme catalyzing the transfer of a sulfo group from a donor cosubstrate, usually 3'-phosphoadenosine-5'-phosphosulfate (PAPS), to a substrate molecule's hydroxyl or amine, resulting in a sulfate or sulfamate, respectively. Sulfation is involved in a variety of biological processes, including detoxification, hormone regulation, molecular recognition, cell signaling, and viral entry into cells.[1] It is among the reactions in phase II drug metabolism, frequently effective in rendering a xenobiotic less active from a pharmacological and toxicological standpoint, but sometimes playing a role in the activation of xenobiotics (e.g. aromatic amines, methyl-substituted polycyclic aromatic hydrocarbons). Another example of biological sulfation is in the synthesis of sulfonated glycosaminoglycans, such as heparin, heparan sulfate, chondroitin sulfate, and dermatan sulfate. Sulfation is also a possible posttranslational modification of proteins.
Examples
Sulfation occurs as a part of several important biological processes.
Tyrosine sulfation
Tyrosine sulfation is a posttranslational modification in which a tyrosine residue of a protein is sulfated by a tyrosylprotein sulfotransferase (TPST) typically in the Golgi apparatus. Secreted proteins and extracellular parts of membrane proteins that pass through the Golgi apparatus may be sulfated. Such sulfation was first discovered by Bettelheim in bovine fibrinopeptide B in 1954[2] and later found be present in animals and plants but not in prokaryotes or in yeasts. Sulfation sites are tyrosine residues exposed on the surface of the protein typically surrounded by acidic residues. A detailed description of the characteristics of the sulfation site is available from PROSITE (PROSITE pattern: PS00003)[1]. Two types of tyrosylprotein sulfotransferases (TPST-1 and TPST-2) have been identified. Recently identified RaxX protein from most Xanthomonas species contains tyrosine sulfation residue, and mimics the plant peptide hormone PSY (Amano et al., 2007, Pruitt et al., 2015, 2017).
Function of tyrosine sulfation
Sulfation plays role in strengthening protein–protein interactions. Types of human proteins known to undergo tyrosine sulfation include adhesion molecules, G-protein-coupled receptors, coagulation factors, serine protease inhibitors, extracellular matrix proteins, and hormones. Tyrosine O-sulfate is a stable molecule and is excreted in urine in animals. No enzymatic mechanism of tyrosine sulfate desulfation is known to exist. By knock-out of TPST genes in mice, it may be observed that tyrosine sulfation has effects on the growth of the mice, such as body weight, fecundity, and postnatal viability.
Regulation of tyrosine sulfation
There is very limited evidence that the TPST genes are subject to transcriptional regulation and tyrosine O-sulfate is very stable and cannot be easily degraded by mammalian sulfatases. Tyrosine O-sulfation is an irreversible process in vivo. An antibody called PSG2 shows high sensitivity and specificity for epitopes containing sulfotyrosine independent of the sequence context. New tools are being developed to study TPST's, using synthetic peptides and small molecule screens.[3]
Seagrasses
The evolution of several sulfotransferases appears to have facilitated the adaptation of the terrestrial ancestors of seagrasses to a new marine habitat.[4][5]
See also
References
- ^ a b Chapman, Eli; Best, Michael D.; Hanson, Sarah R.; Wong, Chi-Huey (2004-07-05). "Sulfotransferases: Structure, Mechanism, Biological Activity, Inhibition, and Synthetic Utility". Angewandte Chemie International Edition. 43 (27): 3526–3548. doi:10.1002/anie.200300631. ISSN 1521-3773. PMID 15293241.
- ^ Bettelheim, F. R. (1954). "Tyrosine-O-sulfate in a peptide from fibrinogen". J. Am. Chem. Soc. 76 (10): 2838–2839. doi:10.1021/ja01639a073.
- ^ Byrne, D. P. (2018). "New tools for evaluating protein tyrosine sulfation: tyrosylprotein sulfotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors". Biochemical Journal. 475 (15): 2435–2455. doi:10.1042/BCJ20180266.
- ^ Olsen, Jeanine L.; et al. (2016). "The genome of the seagrass Zostera marina reveals angiosperm adaptation to the sea". Nature. 530 (7590): 331–335. Bibcode:2016Natur.530..331O. doi:10.1038/nature16548. PMID 26814964. S2CID 3713147.
- ^ Pfeifer, Lukas; Classen, Birgit (2020). "The Cell Wall of Seagrasses: Fascinating, Peculiar and a Blank Canvas for Future Research". Frontiers in Plant Science. 11: 588754. doi:10.3389/fpls.2020.588754. PMC 7644952. PMID 33193541.
{{cite journal}}: CS1 maint: unflagged free DOI (link)
- Moore KL (2003). "The biology and enzymology of protein tyrosine O-sulfation". J. Biol. Chem. 278 (27): 24243–6. doi:10.1074/jbc.R300008200. PMID 12730193.
- Hoffhines AJ; Damoc, E; Bridges, KG; Leary, JA; Moore, KL (2006). "Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody". J. Biol. Chem. 281 (49): 37877–87. doi:10.1074/jbc.M609398200. PMC 1764208. PMID 17046811.
{{cite journal}}: CS1 maint: unflagged free DOI (link)