Glycoside Hydrolase Family 143 - Revision history

Grete Raba at 22:16, 25 August 2023

2023-08-25T22:16:32Z

Grete Raba at 22:15, 25 August 2023

2023-08-25T22:15:12Z

Grete Raba at 22:07, 25 August 2023

2023-08-25T22:07:51Z

Grete Raba at 21:51, 25 August 2023

2023-08-25T21:51:15Z

Grete Raba at 20:34, 25 August 2023

2023-08-25T20:34:14Z

Grete Raba at 20:19, 25 August 2023

2023-08-25T20:19:31Z

Harry Brumer: added new author Grete Raba

2023-07-04T19:13:54Z

added new author Grete Raba

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

2021-12-18T21:15:33Z

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

Harry Brumer: Ana Luis assigned as RC

2020-06-18T01:39:44Z

Ana Luis assigned as RC

Harry Brumer: Created page with "{{UnassignedPage}} GH143"

2018-02-16T10:16:31Z

Created page with "{{UnassignedPage}} GH143"

New page

{{UnassignedPage}}

[[Category:Glycoside Hydrolase Families|GH143]]

@@ Line 18: / Line 18: @@
 |-
 |'''Active site residues'''
-|known/not known
+|known
 |-
 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''

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 |-
 |'''Mechanism'''
-|retaining/inverting
+|retaining (inferred)
 |-
 |'''Active site residues'''
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 == Kinetics and Mechanism ==
-The structural similarities between BT1020 N-terminus from GH143 and sialidases from GH33, especially in their catalytic apparatuses, suggest a retaining catalytic mechanism <cite>Ndeh2017</cite>. Understanding specific kinetics and mechanisms needs further studies.
+The structural similarities between BT1020 N-terminus from GH143 and sialidases from GH33 suggest a retaining catalytic mechanism <cite>Ndeh2017</cite>. Understanding specific kinetics and mechanisms of GH143 enzymes needs further studies.
 == Catalytic Residues ==

@@ Line 32: / Line 32: @@
 == Kinetics and Mechanism ==
-Content is to be added here.
+The structural similarities between BT1020 N-terminus from GH143 and sialidases from GH33, especially in their catalytic apparatuses, suggest a retaining catalytic mechanism <cite>Ndeh2017</cite>. Understanding specific kinetics and mechanisms needs further studies.
 == Catalytic Residues ==

@@ Line 38: / Line 38: @@
 == Three-dimensional structures ==
-The N-terminus of BT1020 has a 5-bladed β-propeller structure with 2-keto-3-deoxy-D-lyxo-heptulosaric acid (DHA)-hydrolase activity <cite>Ndeh2017</cite>.
+The N-terminus of BT1020 is made of 380 amino acid residues, arranged into 5-bladed β-propeller structure with 2-keto-3-deoxy-D-lyxo-heptulosaric acid (DHA)-hydrolase activity <cite>Ndeh2017</cite>.
 == Family Firsts ==

@@ Line 29: / Line 29: @@
 == Substrate specificities ==
-The members of GH142 family are 1-keto-3-deoxy-D-lyxo-heptulosaric acid (DHA) hydrolases (EC 3.2.1.-). The first characterized enzyme from this family was the N-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. BT1020 cleaves the D-DHA- β-2,3-D-GalA linkage in rhamnogalacturonan II (RG II) in pectin.
+The members of GH142 family are 1-keto-3-deoxy-D-lyxo-heptulosaric acid (DHA) hydrolases ([{{EClink}}3.2.1.- EC 3.2.1.-]). The first characterized enzyme from this family was the N-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. BT1020 cleaves the D-DHA- β-2,3-D-GalA linkage in rhamnogalacturonan II (RG II) in pectin.
 == Kinetics and Mechanism ==

@@ Line 29: / Line 29: @@
 == Substrate specificities ==
-Content is to be added here.
+The members of GH142 family are 1-keto-3-deoxy-D-lyxo-heptulosaric acid (DHA) hydrolases (EC 3.2.1.-). The first characterized enzyme from this family was the N-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. BT1020 cleaves the D-DHA- β-2,3-D-GalA linkage in rhamnogalacturonan II (RG II) in pectin.
 == Kinetics and Mechanism ==
@@ Line 39: / Line 35: @@
 == Catalytic Residues ==
-Content is to be added here.
+The active site of DHA-hydrolase (N-terminus of BT1020) contains tyrosine and glutamate residues that function as the catalytic nucleophile and acid-base residues <cite>Ndeh2017</cite>.
 == Three-dimensional structures ==
-Content is to be added here.
+The N-terminus of BT1020 has a 5-bladed β-propeller structure with 2-keto-3-deoxy-D-lyxo-heptulosaric acid (DHA)-hydrolase activity <cite>Ndeh2017</cite>.
 == Family Firsts ==
-;First stereochemistry determination: Content is to be added here.
+;First stereochemistry determination: Not yet identified.
-;First catalytic nucleophile identification: Content is to be added here.
+;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
-;First general acid/base residue identification: Content is to be added here.
+;First general acid/base residue identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
-;First 3-D structure: Content is to be added here.
+;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
 == References ==
 <biblio>
-#Cantarel2009 pmid=18838391
+#Ndeh2017 pmid=28329766
 </biblio>
 [[Category:Glycoside Hydrolase Families|GH143]]

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 {{UnderConstruction}}
-* [[Author]]: [[User:Ana Luis|Ana Luis]]
+* [[Author]]: [[User:Grete Raba|Grete Raba]]
 * [[Responsible Curator]]:  [[User:Ana Luis|Ana Luis]]
 ----

← Older revision		Revision as of 01:39, 18 June 2020
Line 1:		Line 1:
−	{{~~UnassignedPage~~}}	+	<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
		+	{{UnderConstruction}}
		+	* [[Author]]: ^^^Ana Luis^^^
		+	* [[Responsible Curator]]: ^^^Ana Luis^^^
		+	----

		+	<!-- 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}}
		+	\|-
		+	\|{{Hl2}} colspan="2" align="center" \|'''Glycoside Hydrolase Family GH143'''
		+	\|-
		+	\|'''Clan'''
		+	\|GH-x
		+	\|-
		+	\|'''Mechanism'''
		+	\|retaining/inverting
		+	\|-
		+	\|'''Active site residues'''
		+	\|known/not known
		+	\|-
		+	\|{{Hl2}} colspan="2" align="center" \|'''CAZy DB link'''
		+	\|-
		+	\| colspan="2" \|{{CAZyDBlink}}GH143.html
		+	\|}
		+	</div>
		+	<!-- This is the end of the table -->
		+
		+
		+	== Substrate specificities ==
		+	Content is to be added here.
		+
		+	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...)''
		+
		+	In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
		+
		+	== Kinetics and Mechanism ==
		+	Content is to be added here.
		+
		+	== Catalytic Residues ==
		+	Content is to be added here.
		+
		+	== Three-dimensional structures ==
		+	Content is to be added here.
		+
		+	== Family Firsts ==
		+	;First stereochemistry determination: Content is to be added here.
		+	;First catalytic nucleophile identification: Content is to be added here.
		+	;First general acid/base residue identification: Content is to be added here.
		+	;First 3-D structure: Content is to be added here.
		+
		+	== References ==
		+	<biblio>
		+	#Cantarel2009 pmid=18838391
		+	#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version].
		+	</biblio>

	[[Category:Glycoside Hydrolase Families\|GH143]]		[[Category:Glycoside Hydrolase Families\|GH143]]