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Difference between revisions of "Glycosyltransferase Family 38"
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<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> | <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> | ||
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{{UnderConstruction}} | {{UnderConstruction}} | ||
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* [[Author]]: ^^^Warren Wakarchuk^^^ | * [[Author]]: ^^^Warren Wakarchuk^^^ | ||
| − | * [[Responsible Curator]]: | + | * [[Responsible Curator]]: ^^^Warren Wakarchuk^^^ |
| + | |||
---- | ---- | ||
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --> | <!-- The data in the table below should be updated by the Author/Curator according to current information on the family --> | ||
| − | <div style="float:right"> | + | <div style="float: right"> |
| − | {| {{Prettytable}} | + | {| {{Prettytable}} |
|- | |- | ||
| − | |{{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT38''' | + | | {{Hl2}} colspan="2" align="center" |'''Glycosyltransferase Family GT38''' |
|- | |- | ||
| − | |'''Clan''' | + | | '''Clan''' |
| − | |GT-B | + | | GT-B |
|- | |- | ||
| − | |'''Mechanisn''' | + | | '''Mechanisn''' |
| − | + | | inverting | |
| − | |inverting | ||
| − | |||
|- | |- | ||
| − | |'''Active site residues''' | + | | '''Active site residues''' |
| − | |known | + | | known |
|- | |- | ||
| − | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | + | | {{Hl2}} colspan="2" align="center" |'''CAZy DB link''' |
|- | |- | ||
| colspan="2" |{{CAZyDBlink}}GT38.html | | colspan="2" |{{CAZyDBlink}}GT38.html | ||
|} | |} | ||
</div> | </div> | ||
| + | |||
<!-- This is the end of the table --> | <!-- This is the end of the table --> | ||
| + | == Substrate specificities == | ||
| − | + | Members of GT-38 are the bacterial polysialyltransferases (polySTs), which catalyze the addition of sialic acids from the activated sugar donor, CMP-sialic acid (CMP-Neu5Ac), to the nonreducing end of the growing polySia chain <cite> Cho1994</cite>. These enzymes build the polymer as a capsular polysaccharide on a specialized poly-β-KDO modified lyso-phosphatidyl glycerol anchor in the membrane of Gram negative bacteria ''Willis2013''. . Bacterial polySia capsules exist in three different flavours: ''Escherichia coli'' K1, ''Neisseria meningitidis'' serotype B, ''Moraxella nonliquefaciens'', and ''Mannheimia'' ''haemolytica'' A2 synthesize α-2,8-linked polySia whereas ''N. meningitidis'' serotype C produces a α-2,9-linked polymer and ''E. coli'' K92 produces polymers with alternating α-2,8 and α-2,9 linkages PMID: 10052589 PMID: 1898915 PMID: 64575. The molecular mimicry of these bacterial polySia capsules represents an elegant strategy to evade the host’s immune recognition since they are not considered as foreign. In addition, they confer a physical barrier protecting the pathogen from killing by the complement system PMID: 8884739. | |
| − | Members of GT-38 are the bacterial polysialyltransferases (polySTs), which catalyze the addition of sialic acids from the activated sugar donor, CMP-sialic acid (CMP-Neu5Ac), to the nonreducing end of the growing polySia chain | ||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| + | |||
Content is to be added here. | Content is to be added here. | ||
== Catalytic Residues == | == Catalytic Residues == | ||
| + | |||
Content is to be added here. | Content is to be added here. | ||
== Three-dimensional structures == | == Three-dimensional structures == | ||
| + | |||
Content is to be added here. | Content is to be added here. | ||
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: Content is to be added here. | + | |
| − | ;First catalytic nucleophile identification: Content is to be added here. | + | ; First stereochemistry determination: Content is to be added here. |
| − | ;First general acid/base residue identification: Content is to be added here. | + | ; First catalytic nucleophile identification: Content is to be added here. |
| − | ;First 3-D structure: Content is to be added here. | + | ; First general acid/base residue identification: Content is to be added here. |
| + | ; First 3-D structure: Content is to be added here. | ||
== References == | == References == | ||
| − | |||
| − | |||
| − | |||
| − | #Lizak2017 pmid=28724897 | + | # Cantarel2009 pmid=18838391 |
| − | #Lindhout2013 pmid=23922842 | + | # DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version]. |
| − | #Willis2013 pmid=23610430 | + | |
| − | #Willis2008 pmid=18000029 | + | # Lizak2017 pmid=28724897 |
| − | #Cho1994 pmid=7972078 | + | # Lindhout2013 pmid=23922842 |
| − | #PuentePolledo pmid=10052589 | + | # Willis2013 pmid=23610430 |
| − | #Devi1991 pmid=1898915 | + | # Willis2008 pmid=18000029 |
| − | #Glode1977 pmid=64575 | + | # Cho1994 pmid=7972078 |
| − | + | # PuentePolledo pmid=10052589 | |
| + | # Devi1991 pmid=1898915 | ||
| + | # Glode1977 pmid=64575 | ||
[[Category:Glycosyltransferase Families|GT038]] | [[Category:Glycosyltransferase Families|GT038]] | ||
Revision as of 10:14, 27 May 2020
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Author: ^^^Warren Wakarchuk^^^
- Responsible Curator: ^^^Warren Wakarchuk^^^
| Glycosyltransferase Family GT38 | |
| Clan | GT-B |
| Mechanisn | inverting |
| Active site residues | known |
| CAZy DB link | |
| https://www.cazy.org/GT38.html | |
Substrate specificities
Members of GT-38 are the bacterial polysialyltransferases (polySTs), which catalyze the addition of sialic acids from the activated sugar donor, CMP-sialic acid (CMP-Neu5Ac), to the nonreducing end of the growing polySia chain [1]. These enzymes build the polymer as a capsular polysaccharide on a specialized poly-β-KDO modified lyso-phosphatidyl glycerol anchor in the membrane of Gram negative bacteria Willis2013. . Bacterial polySia capsules exist in three different flavours: Escherichia coli K1, Neisseria meningitidis serotype B, Moraxella nonliquefaciens, and Mannheimia haemolytica A2 synthesize α-2,8-linked polySia whereas N. meningitidis serotype C produces a α-2,9-linked polymer and E. coli K92 produces polymers with alternating α-2,8 and α-2,9 linkages PMID: 10052589 PMID: 1898915 PMID: 64575. The molecular mimicry of these bacterial polySia capsules represents an elegant strategy to evade the host’s immune recognition since they are not considered as foreign. In addition, they confer a physical barrier protecting the pathogen from killing by the complement system PMID: 8884739.
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Content is to be added here.
- First catalytic nucleophile identification
- Content is to be added here.
- First general acid/base residue identification
- Content is to be added here.
- First 3-D structure
- Content is to be added here.
References
- Cantarel2009 pmid=18838391
- DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. Download PDF version.
- Lizak2017 pmid=28724897
- Lindhout2013 pmid=23922842
- Willis2013 pmid=23610430
- Willis2008 pmid=18000029
- Cho1994 pmid=7972078
- PuentePolledo pmid=10052589
- Devi1991 pmid=1898915
- Glode1977 pmid=64575