Carbohydrate Esterase Family 20 - Revision history

Plinio Vieira at 11:42, 23 March 2023

2023-03-23T11:42:53Z

Plinio Vieira at 11:32, 23 March 2023

2023-03-23T11:32:11Z

Plinio Vieira at 11:22, 23 March 2023

2023-03-23T11:22:30Z

Plinio Vieira at 11:17, 23 March 2023

2023-03-23T11:17:06Z

Plinio Vieira at 11:15, 23 March 2023

2023-03-23T11:15:29Z

Plinio Vieira at 19:41, 22 March 2023

2023-03-22T19:41:56Z

Plinio Vieira at 19:41, 22 March 2023

2023-03-22T19:41:06Z

Plinio Vieira at 19:38, 22 March 2023

2023-03-22T19:38:56Z

Plinio Vieira at 19:38, 22 March 2023

2023-03-22T19:38:25Z

Plinio Vieira at 19:33, 22 March 2023

2023-03-22T19:33:22Z

@@ Line 32: / Line 32: @@
 == Catalytic residues ==
-[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent <cite>Vieira2021</cite>, as is expected for other related carbohydrate esterase (CE) families [[CE2]], [[CE3]], [[CE6]], [[CE12]] and [[CE17]] that harbour the SGNH-hydrolase fold.
+[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through Glycine backbone, Block IV is absent <cite>Vieira2021</cite>, as is expected for other related carbohydrate esterase (CE) families [[CE2]], [[CE3]], [[CE6]], [[CE12]] and [[CE17]], that harbour the SGNH-hydrolase fold.
 == Kinetics and Mechanism ==

@@ Line 32: / Line 32: @@
 == Catalytic residues ==
-[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent <cite>Vieira2021</cite>, as noted for other related carbohydrate esterase (CE) families [[CE2]], [[CE3]], [[CE6]], [[CE12]] and [[CE17]].
+[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent <cite>Vieira2021</cite>, as is expected for other related carbohydrate esterase (CE) families [[CE2]], [[CE3]], [[CE6]], [[CE12]] and [[CE17]] that harbour the SGNH-hydrolase fold.
 == Kinetics and Mechanism ==

@@ Line 32: / Line 32: @@
 == Catalytic residues ==
-[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent <cite>Vieira2021</cite>, as noted for other related carbohydrate esterase (CE) families.
+[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent <cite>Vieira2021</cite>, as noted for other related carbohydrate esterase (CE) families [[CE2]], [[CE3]], [[CE6]], [[CE12]] and [[CE17]].
 == Kinetics and Mechanism ==
-''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG <cite>Vieira2021</cite>. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate <cite>Liu2022</cite>.
+''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG. ''Xac''XaeA showed lower activity towards metanoate compared to the prefered substrate acetate, but catalysis was not observed for longer chains <cite>Vieira2021</cite>. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate <cite>Liu2022</cite>.
 == Three-dimensional structures ==

@@ Line 32: / Line 32: @@
 == Catalytic residues ==
-[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent <cite>Vieira2021</cite>, as noted for other related carbohydrate esterase (CE) families.
+[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent <cite>Vieira2021</cite>, as noted for other related carbohydrate esterase (CE) families.
 == Kinetics and Mechanism ==

@@ Line 32: / Line 32: @@
 == Catalytic residues ==
-[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a). Catalytic residues are circled. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps. Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent <cite>Vieira2021</cite>, as noted for other related carbohydrate esterase (CE) families.
+[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent <cite>Vieira2021</cite>, as noted for other related carbohydrate esterase (CE) families.
 == Kinetics and Mechanism ==

@@ Line 31: / Line 31: @@
 Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) <cite>Vieira2021</cite> and acetylesterases putatively related to arabinoxylan deacetylation <cite>Liu2022</cite>.
 == Catalytic residues ==
+[[Image:Ce20_cazypedia.png|thumb|500px|Figure 1: The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a). Catalytic residues are circled. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps. Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent <cite>Vieira2021</cite>, as noted for other related carbohydrate esterase (CE) families.
 == Kinetics and Mechanism ==

← Older revision		Revision as of 19:38, 22 March 2023
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	Carbohydrate esterase family 20 (CE20) currently comprises xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) <cite>Vieira2021</cite> and acetylesterases putatively related to arabinoxylan deacetylation <cite>Liu2022</cite>.		Carbohydrate esterase family 20 (CE20) currently comprises xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) <cite>Vieira2021</cite> and acetylesterases putatively related to arabinoxylan deacetylation <cite>Liu2022</cite>.

		+	[[Image:Ce20_cazypedia.png\|thumb\|500px\|Figure 1: The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a). Catalytic residues are circled. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps. Adapted from <cite>Vieira2021</cite> originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]
	== Catalytic residues ==		== Catalytic residues ==