Glycoside Hydrolase Family 174 - Revision history

Yaoguang Chang at 08:48, 26 May 2023

2023-05-26T08:48:46Z

Guanchen Liu at 01:42, 26 May 2023

2023-05-26T01:42:46Z

Guanchen Liu at 01:39, 26 May 2023

2023-05-26T01:39:20Z

Guanchen Liu at 01:37, 26 May 2023

2023-05-26T01:37:32Z

Guanchen Liu at 01:33, 26 May 2023

2023-05-26T01:33:16Z

Guanchen Liu at 01:32, 26 May 2023

2023-05-26T01:32:28Z

Guanchen Liu at 01:31, 26 May 2023

2023-05-26T01:31:35Z

Guanchen Liu at 01:21, 26 May 2023

2023-05-26T01:21:04Z

Guanchen Liu at 00:59, 26 May 2023

2023-05-26T00:59:32Z

Harry Brumer: added Guanchen Liu as Author

2023-01-06T19:59:50Z

added Guanchen Liu as Author

@@ Line 1: / Line 1: @@
 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
-{{UnderConstruction}}
+{{CuratorApproved}}
 * [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]

@@ Line 31: / Line 31: @@
 == Substrate specificities ==
-Members of [[GH174|glycoside hydrolase family 174]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a processive endo-acting manner.<ref>Liu2023</ref> Meanwhile, three homologs of Fun174A from ''Rubritalea marina'', ''Spartobacteria bacterium'' and ''Wenyingzhuangia fucanilytica'', display activities toward sulfated fucan from ''Isostichopus badionotus''.<ref>Liu2023</ref> All 92 members (up to May,2023) of GH174 are bacterial enzymes.
+Members of [[GH174|glycoside hydrolase family 174]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a processive endo-acting manner.<cite>Liu2023</cite> Meanwhile, three homologs of Fun174A from ''Rubritalea marina'', ''Spartobacteria bacterium'' and ''Wenyingzhuangia fucanilytica'', display activities toward sulfated fucan from ''Isostichopus badionotus''.<cite>Liu2023</cite> All 92 members (up to May,2023) of GH174 are bacterial enzymes.
-[[File:Tree.png|thumb]]
+[[File:Tree.png|thumb|'''Figure 1. The phylogenetic tree of GH174 homologs.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]
 == Kinetics and Mechanism ==
-The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<ref>Liu2023</ref>
+The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<cite>Liu2023</cite>
 == Catalytic Residues ==
-Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from ''Isostichopus badionotus'' respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<ref>Liu2023</ref>
+Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from ''Isostichopus badionotus'' respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<cite>Liu2023</cite>
-[[File:Weblogo.jpg|thumb]]
+[[File:Weblogo.jpg|thumb|'''Figure 2. Multiple sequence alignments of residues in GH174 homologs.''' The highly conserved acidic amino acids in all sequences were indicated with black triangles.]]
 == Three-dimensional structures ==
 No three-dimensional structure has been solved in this glycoside hydrolase family at present.

@@ Line 31: / Line 31: @@
 == Substrate specificities ==
-Members of [[GH174|glycoside hydrolase family 174]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from ''Rubritalea marina'', ''Spartobacteria bacterium'' and ''Wenyingzhuangia fucanilytica'', display activities toward sulfated fucan from ''Isostichopus badionotus''. All 92 members (up to May,2023) of GH174 are bacterial enzymes.
+Members of [[GH174|glycoside hydrolase family 174]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a processive endo-acting manner.<ref>Liu2023</ref> Meanwhile, three homologs of Fun174A from ''Rubritalea marina'', ''Spartobacteria bacterium'' and ''Wenyingzhuangia fucanilytica'', display activities toward sulfated fucan from ''Isostichopus badionotus''.<ref>Liu2023</ref> All 92 members (up to May,2023) of GH174 are bacterial enzymes.
 [[File:Tree.png|thumb]]
 == Kinetics and Mechanism ==
-The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.
+The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<ref>Liu2023</ref>
 == Catalytic Residues ==
-Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from ''Isostichopus badionotus'' respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.
+Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from ''Isostichopus badionotus'' respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<ref>Liu2023</ref>
 [[File:Weblogo.jpg|thumb]]
 == Three-dimensional structures ==

@@ Line 31: / Line 31: @@
 == Substrate specificities ==
-Members of glycoside hydrolase family 174 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium Wenyingzhuangia aestuarii OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from Rubritalea marina, Spartobacteria bacterium and Wenyingzhuangia fucanilytica, display activities toward sulfated fucan from Isostichopus badionotus. All 92 members (up to May,2023) of GH174 are bacterial enzymes.
+Members of [[GH174|glycoside hydrolase family 174]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from ''Rubritalea marina'', ''Spartobacteria bacterium'' and ''Wenyingzhuangia fucanilytica'', display activities toward sulfated fucan from ''Isostichopus badionotus''. All 92 members (up to May,2023) of GH174 are bacterial enzymes.
 [[File:Tree.png|thumb]]
@@ Line 38: / Line 38: @@
 == Catalytic Residues ==
-Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from Isostichopus badionotus respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.
+Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from ''Isostichopus badionotus'' respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.
 [[File:Weblogo.jpg|thumb]]
 == Three-dimensional structures ==

@@ Line 33: / Line 33: @@
 Members of glycoside hydrolase family 174 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium Wenyingzhuangia aestuarii OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from Rubritalea marina, Spartobacteria bacterium and Wenyingzhuangia fucanilytica, display activities toward sulfated fucan from Isostichopus badionotus. All 92 members (up to May,2023) of GH174 are bacterial enzymes.
 [[File:Tree.png|thumb]]
 == Kinetics and Mechanism ==

@@ Line 32: / Line 32: @@
 == Substrate specificities ==
 Members of glycoside hydrolase family 174 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium Wenyingzhuangia aestuarii OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a processive endo-acting manner. Meanwhile, three homologs of Fun174A from Rubritalea marina, Spartobacteria bacterium and Wenyingzhuangia fucanilytica, display activities toward sulfated fucan from Isostichopus badionotus. All 92 members (up to May,2023) of GH174 are bacterial enzymes.
-[[File:Tree.png|thumb]]
+[[File:Tree.png|'''Figure 1. The phylogenetic tree of GH174 homologs.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]
 Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''
@@ Line 42: / Line 42: @@
 == Catalytic Residues ==
 Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from Isostichopus badionotus respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.
-[[File:Weblogo.jpg|thumb]]
+[[File:Weblogo.jpg|'''Figure 2. Multiple sequence alignments of residues in GH174 homologs.''' The highly conserved acidic amino acids in all sequences were indicated with black triangles.]]
 == Three-dimensional structures ==
 No three-dimensional structure has been solved in this glycoside hydrolase family at present.
@@ Line 55: / Line 55: @@
 <biblio>
 #Liu2023 pmid=36746582
 </biblio>
 <!-- Do not delete this Category tag -->
 [[Category:Glycoside Hydrolase Families|GH174]]