Transglycosylases - Revision history

Spencer Williams at 00:58, 2 August 2024

2024-08-02T00:58:06Z

Spencer Williams at 00:40, 2 August 2024

2024-08-02T00:40:51Z

Harry Brumer at 16:54, 12 November 2015

2015-11-12T16:54:15Z

Harry Brumer at 08:01, 18 December 2013

2013-12-18T08:01:34Z

Harry Brumer: /* References */

2013-05-07T01:04:14Z

References

Harry Brumer: fixed-up Vocadlo + Withers reference

2013-05-07T01:03:56Z

fixed-up Vocadlo + Withers reference

Spencer Williams at 20:59, 6 May 2013

2013-05-06T20:59:39Z

Spencer Williams: /* Overview */

2013-05-06T20:58:21Z

Overview

Harry Brumer: /* Families */ removed comma

2013-05-06T17:31:40Z

Families: removed comma

Harry Brumer: /* Overview */ figure & legend reformatted

2013-05-06T17:30:39Z

Overview: figure & legend reformatted

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 *[[GH77]], for examples amylomaltase, which catalyzes the synthesis of maltodextrins from maltose <cite>Maarel2013</cite>.
 *[[GH23]], [[GH102]], [[GH103]], and [[GH104]] lytic transglycosylases, which convert peptidoglycan to 1,6-anhydrosugars <cite>Schuerwater2008</cite>.
 == References ==
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 #Sinnott1990 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]
 #Bissaro2015 pmid=25793417
 </biblio>
 [[Category:Definitions and explanations]]

← Older revision		Revision as of 00:40, 2 August 2024
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	== Overview ==		== Overview ==

−	'''Transglycosylases''' are a class of GH enzymes that can catalyze the transformation of one glycoside to another. That is, these enzymes catalyze the intra- or intermolecular substitution of the anomeric position of a glycoside. Mechanistically, transglycosylases utilize the same mechanism as various [[retaining]] glycoside hydrolases <cite>Sinnott1990 Bissaro2015</cite>. Thus, reaction of the nucleophile of a retaining glycoside hydrolase with a substrate gives a glycosyl-enzyme [[intermediate]] that can be intercepted either by water to give the hydrolysis product, or by another acceptor (often another carbohydrate alcohol), to give a new glycoside or oligosaccharide <cite>Crout1998</cite>. Alternatively, transglycosylation can occur by [[neighboring group participation]], wherein a neighboring 2-acetamido group participates in the reaction to generate an [[oxazolinium ion]] intermediate, which again can react with another acceptor other than water. Some transglycosidases possess substantial [[glycoside hydrolase]] activity, and some glycoside hydrolases possess transglycosylase activity <cite>Vocadlo2000</cite>. Indeed, in many cases it is unclear what the major role of an enzyme that possesses both activities may be. Transglycosylases are [[sequence-based classification\|classified]] as [[glycoside hydrolases]] into various GH families on the basis of sequence similarity.	+	'''Transglycosylases''' (also transglycosidases) are a class of GH enzymes that can catalyze the transformation of one glycoside to another. That is, these enzymes catalyze the intra- or intermolecular substitution of the anomeric position of a glycoside. Mechanistically, transglycosylases utilize the same mechanism as various [[retaining]] glycoside hydrolases <cite>Sinnott1990 Bissaro2015</cite>. Thus, reaction of the nucleophile of a retaining glycoside hydrolase with a substrate gives a glycosyl-enzyme [[intermediate]] that can be intercepted either by water to give the hydrolysis product, or by another acceptor (often another carbohydrate alcohol), to give a new glycoside or oligosaccharide <cite>Crout1998</cite>. Alternatively, transglycosylation can occur by [[neighboring group participation]], wherein a neighboring 2-acetamido group participates in the reaction to generate an [[oxazolinium ion]] intermediate, which again can react with another acceptor other than water. Some transglycosidases possess substantial [[glycoside hydrolase]] activity, and some glycoside hydrolases possess transglycosylase activity <cite>Vocadlo2000</cite>. Indeed, in many cases it is unclear what the major role of an enzyme that possesses both activities may be. Transglycosylases are [[sequence-based classification\|classified]] as [[glycoside hydrolases]] into various GH families on the basis of sequence similarity.

@@ Line 5: / Line 5: @@
 == Overview ==
-'''Transglycosylases''' are a class of GH enzymes that can catalyze the transformation of one glycoside to another. That is, these enzymes catalyze the intra- or intermolecular substitution of the anomeric position of a glycoside. Mechanistically, transglycosylases utilize the same mechanism as various [[retaining]] glycoside hydrolases <cite>Sinnott1990</cite>. Thus, reaction of the nucleophile of a retaining glycoside hydrolase with a substrate gives a glycosyl-enzyme [[intermediate]] that can be intercepted either by water to give the hydrolysis product, or by another acceptor (often another carbohydrate alcohol), to give a new glycoside or oligosaccharide <cite>Crout1998</cite>. Alternatively, transglycosylation can occur by [[neighboring group participation]], wherein a neighboring 2-acetamido group participates in the reaction to generate an [[oxazolinium ion]] intermediate, which again can react with another acceptor other than water. Some transglycosidases possess substantial [[glycoside hydrolase]] activity, and some glycoside hydrolases possess transglycosylase activity <cite>Vocadlo2000</cite>. Indeed, in many cases it is unclear what the major role of an enzyme that possesses both activities may be. Transglycosylases are [[sequence-based classification|classified]] as [[glycoside hydrolases]] into various GH families on the basis of sequence similarity.
+'''Transglycosylases''' are a class of GH enzymes that can catalyze the transformation of one glycoside to another. That is, these enzymes catalyze the intra- or intermolecular substitution of the anomeric position of a glycoside. Mechanistically, transglycosylases utilize the same mechanism as various [[retaining]] glycoside hydrolases <cite>Sinnott1990 Bissaro2015</cite>. Thus, reaction of the nucleophile of a retaining glycoside hydrolase with a substrate gives a glycosyl-enzyme [[intermediate]] that can be intercepted either by water to give the hydrolysis product, or by another acceptor (often another carbohydrate alcohol), to give a new glycoside or oligosaccharide <cite>Crout1998</cite>. Alternatively, transglycosylation can occur by [[neighboring group participation]], wherein a neighboring 2-acetamido group participates in the reaction to generate an [[oxazolinium ion]] intermediate, which again can react with another acceptor other than water. Some transglycosidases possess substantial [[glycoside hydrolase]] activity, and some glycoside hydrolases possess transglycosylase activity <cite>Vocadlo2000</cite>. Indeed, in many cases it is unclear what the major role of an enzyme that possesses both activities may be. Transglycosylases are [[sequence-based classification|classified]] as [[glycoside hydrolases]] into various GH families on the basis of sequence similarity.
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 #Vocadlo2000 Vocadlo, D. J. and Withers, S. G. (2008) Glycosidase-Catalysed Oligosaccharide Synthesis, Chapter 29 in ''Carbohydrates in Chemistry and Biology'', Ernst, B., Hart, G. W. and Sinaý, P., eds., Wiley-VCH Verlag GmbH, Weinheim, Germany. [http://dx.doi.org/10.1002/9783527618255.ch29 DOI:10.1002/9783527618255.ch29]
 #Sinnott1990 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]
 </biblio>
 [[Category:Definitions and explanations]]

@@ Line 5: / Line 5: @@
 == Overview ==
-'''Transglycosylases''' are a class of GH enzymes that can catalyze the transformation of one glycoside to another. That is, these enzymes catalyze the intra- or intermolecular substitution of the anomeric position of a glycoside. Mechanistically, transglycosylases utilize the same mechanism as various [[retaining]] glycoside hydrolases. Thus, reaction of the nucleophile of a retaining glycoside hydrolase with a substrate gives a glycosyl-enzyme [[intermediate]] that can be intercepted either by water to give the hydrolysis product, or by another acceptor (often another carbohydrate alcohol), to give a new glycoside or oligosaccharide <cite>Crout1998</cite>. Alternatively, transglycosylation can occur by [[neighboring group participation]], wherein a neighboring 2-acetamido group participates in the reaction to generate an [[oxazolinium ion]] intermediate, which again can react with another acceptor other than water. Some transglycosidases possess substantial [[glycoside hydrolase]] activity, and some glycoside hydrolases possess transglycosylase activity <cite>Vocadlo2000</cite>. Indeed, in many cases it is unclear what the major role of an enzyme that possesses both activities may be. Transglycosylases are [[sequence-based classification|classified]] as [[glycoside hydrolases]] into various GH families on the basis of sequence similarity.
+'''Transglycosylases''' are a class of GH enzymes that can catalyze the transformation of one glycoside to another. That is, these enzymes catalyze the intra- or intermolecular substitution of the anomeric position of a glycoside. Mechanistically, transglycosylases utilize the same mechanism as various [[retaining]] glycoside hydrolases <cite>Sinnott1990</cite>. Thus, reaction of the nucleophile of a retaining glycoside hydrolase with a substrate gives a glycosyl-enzyme [[intermediate]] that can be intercepted either by water to give the hydrolysis product, or by another acceptor (often another carbohydrate alcohol), to give a new glycoside or oligosaccharide <cite>Crout1998</cite>. Alternatively, transglycosylation can occur by [[neighboring group participation]], wherein a neighboring 2-acetamido group participates in the reaction to generate an [[oxazolinium ion]] intermediate, which again can react with another acceptor other than water. Some transglycosidases possess substantial [[glycoside hydrolase]] activity, and some glycoside hydrolases possess transglycosylase activity <cite>Vocadlo2000</cite>. Indeed, in many cases it is unclear what the major role of an enzyme that possesses both activities may be. Transglycosylases are [[sequence-based classification|classified]] as [[glycoside hydrolases]] into various GH families on the basis of sequence similarity.
@@ Line 33: / Line 33: @@
 #Maarel2013 pmid=23465909
 #Vocadlo2000 Vocadlo, D. J. and Withers, S. G. (2008) Glycosidase-Catalysed Oligosaccharide Synthesis, Chapter 29 in ''Carbohydrates in Chemistry and Biology'', Ernst, B., Hart, G. W. and Sinaý, P., eds., Wiley-VCH Verlag GmbH, Weinheim, Germany. [http://dx.doi.org/10.1002/9783527618255.ch29 DOI:10.1002/9783527618255.ch29]
+#Sinnott1990 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]
 </biblio>
 [[Category:Definitions and explanations]]

@@ Line 32: / Line 32: @@
 #Schuerwater2008 pmid=17468031
 #Maarel2013 pmid=23465909
-#Vocadlo2000 Vocadlo, D. J. and Withers, S. G. (2008) Glycosidase-Catalysed Oligosaccharide Synthesis, Chpater 29 in ''Carbohydrates in Chemistry and Biology'', Ernst, B., Hart, G. W. and Sinaý, P., eds., Wiley-VCH Verlag GmbH, Weinheim, Germany. [http://dx.doi.org/10.1002/9783527618255.ch29 DOI:10.1002/9783527618255.ch29]
+#Vocadlo2000 Vocadlo, D. J. and Withers, S. G. (2008) Glycosidase-Catalysed Oligosaccharide Synthesis, Chapter 29 in ''Carbohydrates in Chemistry and Biology'', Ernst, B., Hart, G. W. and Sinaý, P., eds., Wiley-VCH Verlag GmbH, Weinheim, Germany. [http://dx.doi.org/10.1002/9783527618255.ch29 DOI:10.1002/9783527618255.ch29]
 </biblio>
 [[Category:Definitions and explanations]]

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 *[[GH2]], for example LacZ &beta;-galactosidase converts lactose to allolactose <cite>Juers2012</cite>.<br>
 *[[GH13]], for example cyclodextran glucanotransferases that convert linear amylose to cyclodextrins <cite>Uitdehaag1999</cite>; glycogen debranching enzyme, which transfers three glucose residues from the four-residue glycogen branch to a nearby branch <cite>Braun1996</cite>; and trehalose synthase, which catalyzes the interconversion of maltose and trehalose <cite>Zhang2011</cite>.<br>
-*[[GH16]], for example xyloglucan endotransglycosylases, which cuts and rejoins xyloglucan chains in the plant cell wall <cite>Rose2002</cite>.
+*[[GH16]], for example xyloglucan endotransglycosylases, which cuts and rejoins xyloglucan chains in the plant cell wall <cite>Eklof2010</cite>.
 *[[GH31]], for example &alpha;-transglucosidases, which catalyze the transfer of individual glucosyl residues between &alpha;-(1→4)-glucans <cite>Larsbrink2012</cite>.
 *[[GH70]], for example glucansucrases, which catalyse the synthesis of high molecular weight glucans, from sucrose <cite>Hijum2006</cite>.
@@ Line 25: / Line 25: @@
 #Larsbrink2012 pmid=23132856
 #Juers2012 pmid=23011886
-#Rose2002 pmid=12514239
+#Eklof2010 pmid=20421457
 #Braun1996 pmid=8611536
 #Uitdehaag1999 pmid=10331869

← Older revision		Revision as of 20:58, 6 May 2013
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	== Overview ==		== Overview ==

−	'''Transglycosylases''' are a class of GH enzymes that can catalyze the transformation of one glycoside to another. That is, these enzymes catalyze the substitution of a glycoside ~~with another aglycon~~. Mechanistically, transglycosylases utilize the same mechanism as various [[retaining]] glycoside hydrolases. Thus, reaction of the nucleophile of a retaining glycoside hydrolase with a substrate gives a glycosyl-enzyme [[intermediate]] that can be intercepted either by water to give the hydrolysis product, or by another acceptor (often another carbohydrate alcohol), to give a new glycoside or oligosaccharide <cite>Crout1998</cite>. Alternatively, transglycosylation can occur by [[neighboring group participation]], wherein a neighboring 2-acetamido group participates in the reaction to generate an [[oxazolinium ion]] intermediate, which again can react with another acceptor other than water. Some transglycosidases possess substantial [[glycoside hydrolase]] activity, and some glycoside hydrolases possess transglycosylase activity <cite>Vocadlo2000</cite>. Indeed, in many cases it is unclear what the major role of an enzyme that possesses both activities may be. Transglycosylases are [[sequence-based classification\|classified]] as [[glycoside hydrolases]] into various GH families on the basis of sequence similarity.	+	'''Transglycosylases''' are a class of GH enzymes that can catalyze the transformation of one glycoside to another. That is, these enzymes catalyze the intra- or intermolecular substitution of the anomeric position of a glycoside. Mechanistically, transglycosylases utilize the same mechanism as various [[retaining]] glycoside hydrolases. Thus, reaction of the nucleophile of a retaining glycoside hydrolase with a substrate gives a glycosyl-enzyme [[intermediate]] that can be intercepted either by water to give the hydrolysis product, or by another acceptor (often another carbohydrate alcohol), to give a new glycoside or oligosaccharide <cite>Crout1998</cite>. Alternatively, transglycosylation can occur by [[neighboring group participation]], wherein a neighboring 2-acetamido group participates in the reaction to generate an [[oxazolinium ion]] intermediate, which again can react with another acceptor other than water. Some transglycosidases possess substantial [[glycoside hydrolase]] activity, and some glycoside hydrolases possess transglycosylase activity <cite>Vocadlo2000</cite>. Indeed, in many cases it is unclear what the major role of an enzyme that possesses both activities may be. Transglycosylases are [[sequence-based classification\|classified]] as [[glycoside hydrolases]] into various GH families on the basis of sequence similarity.

← Older revision		Revision as of 17:30, 6 May 2013
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−	[[Image:transglycosylation.png\|600px\|~~center]]~~	+	[[Image:transglycosylation.png\|thumb\|center\|600px\|'''Figure. Generalized mechanism of a transglycosylase.''' Enzymatic cleavage of a substrate through a [[classical Koshland retaining mechanism]] results in formation of a glycosyl enzyme intermediate. This can partition to react with either water to cause hydrolysis ([[glycoside hydrolase]] activity) or to an alternative acceptor, often a sugar, to cause transglycosylation (transglycosylase activity).]]
−	~~<center>~~'''Generalized mechanism of a transglycosylase. Enzymatic cleavage of a substrate through a [[classical Koshland retaining mechanism]] results in formation of a glycosyl enzyme intermediate. This can partition to react with either water to cause hydrolysis (glycoside hydrolase activity) or to an alternative acceptor, often a sugar, to cause transglycosylation (transglycosylase activity).~~'''</center>~~

	===Families===		===Families===