Glycoside Hydrolase Family 145 - Revision history

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

2021-12-18T21:15:33Z

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

Harry Brumer: added PMIDs

2021-08-11T20:54:31Z

added PMIDs

Harry Brumer at 18:07, 28 July 2021

2021-07-28T18:07:55Z

Harry Brumer at 18:07, 28 July 2021

2021-07-28T18:07:01Z

Harry Brumer at 18:01, 28 July 2021

2021-07-28T18:01:43Z

Harry Brumer at 17:59, 28 July 2021

2021-07-28T17:59:45Z

Harry Brumer at 17:44, 28 July 2021

2021-07-28T17:44:57Z

Harry Brumer: /* Catalytic Residues */

2020-05-12T15:20:00Z

Catalytic Residues

Alan Cartmell at 08:22, 12 May 2020

2020-05-12T08:22:16Z

Alan Cartmell at 08:20, 12 May 2020

2020-05-12T08:20:24Z

@@ Line 1: / Line 1: @@
-* [[Author]]: ^^^Harry Brumer^^^
+* [[Author]]: [[User:Harry Brumer|Harry Brumer]]
-* [[Responsible Curator]]: ^^^Bernard Henrissat^^^
+* [[Responsible Curator]]: [[User:Bernard Henrissat|Bernard Henrissat]]
 ----

@@ Line 10: / Line 10: @@
 === GH145 is a deleted family ===
-This family has been reclassified as [[Polysaccharide Lyase Family 42]]. Two members of the family from ''Bacteroides'' species were originally shown to have hydrolase activity catalyzed by a semi-conserved active site on the posterior side of the beta-propeller structure <cite>MunozMunoz2017</cite>.  Subsequently, lyase activity on alpha-L-Rha-1,4-alpha-D-GlcA via a well-conserved active site on the anterior surface, with strong similarity to [[PL24]] and [[PL25]], was demonstrated in bacterial <cite>MunozMunoz2021</cite> and fungal <cite>Kondo2021</cite> homologs.
+This family has been reclassified as [[Polysaccharide Lyase Family 42]]. Two members of the family from ''Bacteroides'' species were originally shown to have hydrolase activity catalyzed by a semi-conserved active site on the posterior side of the beta-propeller structure <cite>MunozMunoz2017</cite>.  Subsequently, lyase activity on alpha-L-Rha-1,4-alpha-D-GlcA via a well-conserved active site on the anterior surface, with strong similarity to [[PL24]] and [[PL25]], was demonstrated in fungal <cite>Kondo2021</cite> and bacterial <cite>MunozMunoz2021</cite>  homologs.
 '''References'''
 <biblio>
 #MunozMunoz2017 pmid=28396425
-#MunozMunoz2021 pmid=
+#MunozMunoz2021 pmid=34340552
-#Kondo2021 pmid=
+#Kondo2021 pmid=34303708
 </biblio>
 <!-- The data in the table below should be updated by the Author/Curator according to current information on the family -->

← Older revision		Revision as of 18:07, 28 July 2021
Line 1:		Line 1:
		+	* [[Author]]: ^^^Harry Brumer^^^
		+
	* [[Responsible Curator]]: ^^^Bernard Henrissat^^^		* [[Responsible Curator]]: ^^^Bernard Henrissat^^^
		+
	----		----

@@ Line 7: / Line 7: @@
 === GH145 is a deleted family ===
-This family has been reclassified as [[Polysaccharide Lyase Family 42]]. Members of the family were originally shown to have hydrolase activity catalyzed by a semi-conserved active site on the posterior side of the beta-propeller structure <cite>MunozMunoz2017</cite>.  Subsequently, lyase activity on alpha-L-Rha-1,4-alpha-D-GlcA via a well-conserved active site on the anterior surface, with strong similarity to [[PL24]] and [[PL25]], was demonstrated in bacterial <cite>MunozMunoz2021</cite> and fungal <cite>Kondo2021</cite> homologs.
+This family has been reclassified as [[Polysaccharide Lyase Family 42]]. Two members of the family from ''Bacteroides'' species were originally shown to have hydrolase activity catalyzed by a semi-conserved active site on the posterior side of the beta-propeller structure <cite>MunozMunoz2017</cite>.  Subsequently, lyase activity on alpha-L-Rha-1,4-alpha-D-GlcA via a well-conserved active site on the anterior surface, with strong similarity to [[PL24]] and [[PL25]], was demonstrated in bacterial <cite>MunozMunoz2021</cite> and fungal <cite>Kondo2021</cite> homologs.
 '''References'''

@@ Line 7: / Line 7: @@
 === GH145 is a deleted family ===
-This family has been reclassified as [[Polysaccharide Lyase Family 42]]. Members of the family were originally shown to have hydrolase activity catalyzed by an active site on the posterior side of the beta-propeller structure <cite>MunozMunoz2017</cite>.  Subsequently, lyase activity on alpha-L-Rha-1,4-alpha-D-GlcA via a well-conserved active site on the anterior surface, with strong similarity to [[PL24]] and [[PL25]] was demonstrated in bacterial and fungal homologs.
+This family has been reclassified as [[Polysaccharide Lyase Family 42]]. Members of the family were originally shown to have hydrolase activity catalyzed by a semi-conserved active site on the posterior side of the beta-propeller structure <cite>MunozMunoz2017</cite>.  Subsequently, lyase activity on alpha-L-Rha-1,4-alpha-D-GlcA via a well-conserved active site on the anterior surface, with strong similarity to [[PL24]] and [[PL25]], was demonstrated in bacterial <cite>MunozMunoz2021</cite> and fungal <cite>Kondo2021</cite> homologs.
 '''References'''
 <biblio>
 #MunozMunoz2017 pmid=28396425
 #MunozMunoz2021 pmid=
 #Kondo2021 pmid=

@@ Line 1: / Line 1: @@
-<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
+* [[Responsible Curator]]: ^^^Bernard Henrissat^^^
 {{CuratorApproved}}
-* [[Author]]: ^^^Alan Cartmell^^^
+{{DeletedFamily}}
-* [[Responsible Curator]]:  ^^^Alan Cartmell^^^
-----
+=== GH145 is a deleted 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">
+{| {{Prettytable}}
 |-
-| '''Mechanism'''
+|{{Hl2}} colspan="2" align="center" |'''CAZy DB links'''
 |-
 | colspan="2" |{{CAZyDBlink}}GH145.html
-</div>
+|-
 <!-- This is the end of the table -->
 [[Category:Glycoside Hydrolase Families|GH145]]

@@ Line 36: / Line 36: @@
 == Catalytic Residues ==
-A single catalytic histidine, His48 in BT3686, has been shown to be critical for activity. This was the only residue mutated (to Gln, Ala and Gly) that caused loss of activity and is thought to act as an acid/base. Several homologues of BT3686 exist, which although >80 % identical are inactive due to having Gln at the equivalent position to His48 in BT3686. The introduction of a histidine at into related enzymes BACINT_00347 and BACCELL_00856, from ''bacteroides intestinalis'' and ''bacteroides cellulosilyticus'', generating the mutants Q48H in both proteins, is sufficient to introduce rhamnosidase activity into these, otherwise inactive, enzymes <cite>Munoz-Munoz2017</cite>. No second catalytic residue to could be identified and it was tentatively proposed that the glucurnonic acid participates as a second acid/base residue, portonating its own O4 and activating a water molecule.
+A single catalytic histidine, His48 in BT3686, has been shown to be critical for activity. This was the only residue mutated (to Gln, Ala and Gly) that caused loss of activity and is thought to act as an acid/base. Several homologues of BT3686 exist, which although >80 % identical are inactive due to having Gln at the equivalent position to His48 in BT3686. The introduction of a histidine at into related enzymes BACINT_00347 and BACCELL_00856, from ''Bacteroides intestinalis'' and ''Bacteroides cellulosilyticus'', generating the mutants Q48H in both proteins, is sufficient to introduce rhamnosidase activity into these, otherwise inactive, enzymes <cite>Munoz-Munoz2017</cite>. No second catalytic residue to could be identified and it was tentatively proposed that the glucurnonic acid participates as a second acid/base residue, portonating its own O4 and activating a water molecule.
 == Three-dimensional structures ==