Carbohydrate Esterase Family 1 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:17:38Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Harry Brumer: Changed "Clan" to "fold" in table header

2021-04-06T15:38:47Z

Changed "Clan" to "fold" in table header

Harry Brumer: Updated to Curator Approved

2020-05-06T16:34:13Z

Updated to Curator Approved

Harry Brumer at 16:33, 6 May 2020

2020-05-06T16:33:18Z

Harry Brumer at 16:32, 6 May 2020

2020-05-06T16:32:08Z

Harry Brumer at 16:30, 6 May 2020

2020-05-06T16:30:24Z

Harry Brumer at 16:14, 6 May 2020

2020-05-06T16:14:11Z

Harry Brumer at 16:07, 6 May 2020

2020-05-06T16:07:19Z

Casper Wilkens at 13:18, 6 May 2020

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Casper Wilkens at 13:17, 6 May 2020

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 {{CuratorApproved}}
-* [[Author]]: ^^^Casper Wilkens^^^
+* [[Author]]: [[User:Casper Wilkens|Casper Wilkens]]
-* [[Responsible Curator]]: ^^^Harry Brumer^^^
+* [[Responsible Curator]]: [[User:Harry Brumer|Harry Brumer]]
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 |{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''
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-|'''Clan'''
+|'''Fold'''
 |α/β/α-sandwich
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-<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
+{{CuratorApproved}}
 * [[Author]]: ^^^Casper Wilkens^^^
 * [[Responsible Curator]]: ^^^Harry Brumer^^^

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 == Family Firsts ==
-;First characterized: Experiments published in a patent application in 1992 showed that an enzyme from ''Trichoderma reesei'' later classified as a CE1 enzyme was able to deacetylate xylans <cite>EP0507369A2</cite>. Prior the publication of sequence data in this patent application, the purification and characterization of native fungal acetylxylan esterases was reported <cite>Poutanen1990 Biely1988</cite>. In 2000 more comprehensive characterizations than in above mentioned patent of two CE1 enzymes were published for a cinnamoyl esterase from ''Penicillium funiculosum'' <cite>Kroon2000</cite> and a mycolyltransferase from ''Mycobacterium'' ''tuberculosis'' <cite>Ronning2000</cite>.
+;First characterized: Experiments published in a patent application in 1992 showed that an enzyme from ''Trichoderma reesei'' later classified as a CE1 enzyme was able to deacetylate xylans <cite>EP0507369A2</cite>. Prior the publication of sequence data in this patent application, the purification and characterization of native fungal acetylxylan esterases was reported <cite>Poutanen1990 Biely1988</cite>. In 2000 more comprehensive characterizations of two CE1 enzymes were published for a cinnamoyl esterase from ''Penicillium funiculosum'' <cite>Kroon2000</cite> and a mycolyltransferase from ''Mycobacterium tuberculosis'' <cite>Ronning2000</cite>.
-;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.
+;First mechanistic insight: The crystal structure of ''Mycobacterium tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.
 ;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000   <cite>Ronning2000</cite>.

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 #Kroon2000 pmid=11082184
 #Wefers2017 pmid=28669823
 #EP0507369A2 L.H. De Graff, et al. (1992) Cloning, expression and use of acetyl xylan esterases from fungal origin. [https://patents.google.com/patent/EP0507369A2 EP0507369A2]
-#Poutanen1990 Poutanen, K., Sundberg, M., Korte, H., Puls, J.(1990) Deacetylation of xylans by acetyl esterases of ''Trichoderma reesei''. ''Appl. Microbiol. Biotechnol'', 33, 506–510. [https://dx.doi.org/10.1007/BF00172542 DOI:10.1007/BF00172542]
+#Poutanen1990 Poutanen, K., Sundberg, M., Korte, H., Puls, J.(1990) Deacetylation of xylans by acetyl esterases of ''Trichoderma reesei''. ''Appl Microbiol Biotechnol'', '''33''', 506–510. [https://dx.doi.org/10.1007/BF00172542 DOI:10.1007/BF00172542]
-#Biely1988 Biely, P., MacKenzie, C.R., Schneider, H. (1988) Production of acetyl xylan esterase by ''Trichoderma reesei'' and ''Schizophyllum commune''.  ''Canadian Journal of Microbiology'', 34, 767-772. [https://dx.doi.org/10.1139/m88-130 DOI:10.1139/m88-130]
+#Biely1988 Biely, P., MacKenzie, C.R., Schneider, H. (1988) Production of acetyl xylan esterase by ''Trichoderma reesei'' and ''Schizophyllum commune''.  ''Canadian Journal of Microbiology'', '''34''', 767-772. [https://dx.doi.org/10.1139/m88-130 DOI:10.1139/m88-130]
 </biblio>
 [[Category:Carbohydrate Esterase Families|CE001]]

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 == Catalytic Residues ==
-The catalytic serine is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called "nucleophilic elbow", which serves as a fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine is also conserved <cite>Schubot2001 Prates2001</cite>, while the [[general acid]] may be an aspartic acid or glutamic acid <cite>Holck2019</cite>.
+The catalytic serine is located at the center of a conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called "nucleophilic elbow", which serves as a fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine is also conserved <cite>Schubot2001 Prates2001</cite>, while the [[general acid]] may be an aspartic acid or glutamic acid, as introduced above <cite>Holck2019</cite>.
 == Three-dimensional structures ==
-CE1 is a member of the α/β-hydrolase superfamily <cite>Ronning2000</cite> or refered to as an α/β/α-sandwich, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. A number of CE1 feruloyl esterases have a [[CBM48]] appended that proved to be essential for feruloyl esterase activity on polymeric xylan <cite>Holck2019</cite>, however, there are examples of CE1 feruloyl esterases lacking a CBM that act on polymeric xylan <cite>Wefers2017</cite>.
+The tertiary structure of CE1 members is an α/β/α-sandwich, comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>, placing CE1 within the α/β-hydrolase superfamily <cite>Ronning2000</cite>. A number of CE1 feruloyl esterases have a [[CBM48]] appended that is essential for feruloyl esterase activity on polymeric xylan in some members <cite>Holck2019</cite>.  However, there are also examples of CE1 feruloyl esterases lacking a CBM that act on polymeric xylan <cite>Wefers2017</cite>.
 == Family Firsts ==
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 #Prates2001 pmid=11738044
 #Schubot2001 pmid=11601976
-           #Holck2019 pmid=31558605
+#Holck2019 pmid=31558605
 #Kroon2000 pmid=11082184
 #Wefers2017 pmid=28669823</biblio>
 [[Category:Carbohydrate Esterase Families|CE001]]

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 == Substrate specificities ==
-Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.
+Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families, which comprises acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]), and others <cite>Lombard2014</cite>.
 == Kinetics and Mechanism ==
-CE1 enzymes target a large variety of substrates, however, all appear to utilize the canonical serine hydrolase mechanism, involving a catalytic triad comprising a nucleophilic serine, a histidine, and an acidic amino acid  <cite>Schubot2001 Prates2001</cite>. Both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite>.  After substrate binding, the serine is activated by the proton relay consisting of the histidine and the acid residue, which facilitates nucleophilic attack of the carbonyl carbon atom of the substrate.  This results in the formation of a covalent acyl-enzyme intermediate via a tetrahedral transition state (sometimes known as the "tetrahedral intermediate"), which is stabilized through interactions with two main-chain NH groups in the "oxyanion hole." Following release of the corresponding alcohol as the first product, the acyl-enzyme intermediate is hydrolyzed by the near-microscopic reverse of the first step, with water, activated by the proton relay, acting as the nucleophile <cite>Schubot2001 Prates2001</cite>.
+CE1 enzymes target a large variety of substrates, however, all appear to utilize the canonical serine hydrolase mechanism, involving a catalytic triad comprising a nucleophilic serine, a histidine, and an acidic amino acid <cite>Schubot2001 Prates2001</cite>. Both aspartic and glutamic acid are commonly observed in this position <cite>Holck2019</cite>.  After substrate binding, the serine is activated by the proton relay consisting of the histidine and the acid residue, which facilitates nucleophilic attack on the carbonyl carbon atom of the substrate.  This results in the formation of a covalent acyl-enzyme intermediate via a tetrahedral transition state (sometimes known as the "tetrahedral intermediate"), which is stabilized through interactions with two main-chain NH groups in the "oxyanion hole." Following release of the corresponding alcohol as the first product, the acyl-enzyme intermediate is hydrolyzed by the near-microscopic reverse of the first step, with water, activated by the proton relay, acting as the nucleophile <cite>Schubot2001 Prates2001</cite>.
 == Catalytic Residues ==