CAZypedia - User contributions [en-ca]

Polysaccharide Lyase Family 20

2014-08-07T11:09:35Z

Naotake Konno:

{{UnderConstruction}}
* [[Author]]: ^^^Naotake Konno^^^
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL20'''
|-
|'''Mechanism'''
|β-elimination
|-
|'''Metal Cofactor'''
|calcium
|-
|'''Active site residues'''
|unknown
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}PL20.html
|}
</div>


== Substrate specificities ==
Polysaccharide lyases of family 20 cleave β-1,4 linkages in polyglucuronate (β-1,4-glucuronan lyase; EC 4.2.2.14). The first PL20 enzyme was cloned from filamentous fungus ''Trichoderma reesei'' (TrGL) <cite>Konno2009a</cite>. TrGL was highly specific for β-1,4-glucuronan prepared from regenerated cellulose by 2,2,6,6-tetramethylpiperidine-1-oxyl radical (TEMPO) mediated oxidation (cellouronate).

== Kinetics and Mechanism ==
A PL20 enzyme, TrGL, has been characterized as a β-1,4-glucuronan lyase. TrGL catalyzed depolymerization of β-1,4-glucuronan endolytically by β-elimination <cite>Konno2009a</cite> The enzyme was most active at pH 6.5 and 50 °C, and its activity and thermostability increased in the presence of calcium ions.

== Catalytic Residues ==
There are approximately 40 completely conserved amino-acid residues in the PL20 members <cite>Konno2009b</cite> Possible catalytic residues has been predicted based on structural comparison between TrGL and PL7 alginate lyase A1–II’ <cite>Konno2009b</cite> <cite>Ogura2008</cite>. It seemed to be that the charge neutralizer, the catalytic base and the catalytic acid in the TrGL are Gln91, His53 and Tyr200, respectively. However, in order to clarify the substrate recognition mechanism and the identity of the catalytic residues of PL20, further studies will be required.

== Three-dimensional structures ==
The structure of the TrGL was the first PL20 structure to be reported <cite>Konno2009b</cite>. TrGL has a typical β-jelly roll fold (2ZZJ, 1.8 Å).

== Family Firsts ==
;First First catalytic activity: TrGl from ''Trichoderma reesei'' <cite>Konno2009a</cite>
;First 3-D structure: TrGl from ''Trichoderma reesei'' <cite>Konno2009b</cite>

== References ==
<biblio>
#Konno2009a pmid=18978091
#Konno2009b pmid=19306878
#Ogura2008 pmid=18514736
</biblio>

[[Category:Polysaccharide Lyase Families|PL020]]

Polysaccharide Lyase Family 20

2014-08-07T11:03:50Z

Naotake Konno:

{{UnderConstruction}}
* [[Author]]: ^^^Naotake Konno^^^
* [[Responsible Curator]]: ^^^Shinya Fushinobu^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL20'''
|-
|'''Mechanism'''
|β-elimination
|-
|'''Metal Cofactor'''
|calcium
|-
|'''Active site residues'''
|unknown
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}PL20.html
|}
</div>


== Substrate specificities ==
Polysaccharide lyases of family 20 cleave &beta-1,4 linkages in polyglucuronate (&beta-1,4-glucuronan lyase; EC 4.2.2.14). The first PL20 enzyme was cloned from filamentous fungus ''Trichoderma reesei'' (TrGL) <cite>Konno2009a</cite>. TrGL was highly specific for &beta-1,4-glucuronan prepared from regenerated cellulose by 2,2,6,6-tetramethylpiperidine-1-oxyl radical (TEMPO) mediated oxidation (cellouronate).

== Kinetics and Mechanism ==
A PL20 enzyme, TrGL, has been characterized as a &beta-1,4-glucuronan lyase. TrGL catalyzed depolymerization of &beta-1,4-glucuronan endolytically by &beta-elimination <cite>Konno2009a</cite> The enzyme was most active at pH 6.5 and 50 °C, and its activity and thermostability increased in the presence of calcium ions.

== Catalytic Residues ==
There are approximately 40 completely conserved amino-acid residues in the PL20 members <cite>Konno2009b</cite> Possible catalytic residues has been predicted based on structural comparison between TrGL and PL7 alginate lyase A1–II’ <cite>Konno2009b</cite> <cite>Ogura2008</cite>. It seemed to be that the charge neutralizer, the catalytic base and the catalytic acid in the TrGL are Gln91, His53 and Tyr200, respectively. However, in order to clarify the substrate recognition mechanism and the identity of the catalytic residues of PL20, further studies will be required.

== Three-dimensional structures ==
The structure of the TrGL was the first PL20 structure to be reported <cite>Konno2009b</cite>. TrGL has a typical &beta-jelly roll fold (2ZZJ, 1.8 Å).

== Family Firsts ==
;First First catalytic activity: TrGl from ''Trichoderma reesei'' <cite>Konno2009a</cite>
;First 3-D structure: TrGl from ''Trichoderma reesei'' <cite>Konno2009b</cite>

== References ==
<biblio>
#Konno2009a pmid=18978091
#Konno2009b pmid=19306878
#Ogura2008 pmid=18514736
</biblio>

[[Category:Polysaccharide Lyase Families|PL020]]

User:Naotake Konno

2014-08-07T05:15:12Z

Naotake Konno:

----

[[File:Konno2.png|200px|right]]
Naotake Konno is an associate professor at Department of Applied Biological Chemistry, Utsunomiya University, Japan. He obtained Ph. D. from Graduate School of The University of Tokyo in 2009. He contributed isolation and enzymatic characterization of polysaccharide lyase and glycoside hydrolase belonging new families (PL20, GH128) <cite>Konno2009a</cite> <cite>Konno2009b</cite> <cite>Sakamoto2011</cite>. His research currently focuses on various carbohydrate-active enzymes acting on fungal cell walls, such as chitinases <cite>Konno2012</cite>, beta-1,3-glucanases <cite>Sakamoto2011</cite> and beta-1,6-glucanases <cite>Konno2011</cite>. Some of these enzymes are involved in fungal morphological changes.

----

<biblio>
#Konno2009a pmid=18978091
#Konno2009b pmid=19306878
#Sakamoto2011 pmid=21965406
#Konno2012 pmid=22656067
#Konno2011 pmid=21523473
</biblio>

[[Category:Contributors|Konno,Naotake]]

File:Konno2.png

2014-08-07T05:14:42Z

Naotake Konno:

User:Naotake Konno

2014-08-07T05:08:50Z

Naotake Konno:

----

[[File:Konno.png|200px|right]]
Naotake Konno is an associate professor at Department of Applied Biological Chemistry, Utsunomiya University, Japan. He obtained Ph. D. from Graduate School of The University of Tokyo in 2009. He contributed isolation and enzymatic characterization of polysaccharide lyase and glycoside hydrolase belonging new families (PL20, GH128) <cite>Konno2009a</cite> <cite>Konno2009b</cite> <cite>Sakamoto2011</cite>. His research currently focuses on various carbohydrate-active enzymes acting on fungal cell walls, such as chitinases <cite>Konno2012</cite>, beta-1,3-glucanases <cite>Sakamoto2011</cite> and beta-1,6-glucanases <cite>Konno2011</cite>. Some of these enzymes are involved in fungal morphological changes.

----

<biblio>
#Konno2009a pmid=18978091
#Konno2009b pmid=19306878
#Sakamoto2011 pmid=21965406
#Konno2012 pmid=22656067
#Konno2011 pmid=21523473
</biblio>

[[Category:Contributors|Konno,Naotake]]

File:Konno.png

2014-08-07T05:07:47Z

Naotake Konno:

File:Konno.pdf

2014-08-07T05:00:33Z

Naotake Konno: Naotake Konno uploaded a new version of "File:Konno.pdf": Reverted to version as of 04:52, 7 August 2014

File:Konno.pdf

2014-08-07T05:00:14Z

Naotake Konno: Naotake Konno uploaded a new version of "File:Konno.pdf"

User:Naotake Konno

2014-08-07T04:57:13Z

Naotake Konno:

----

[[File:Konno.pdf|200px|right]]
Naotake Konno is an associate professor at Department of Applied Biological Chemistry, Utsunomiya University, Japan. He obtained Ph. D. from Graduate School of The University of Tokyo in 2009. He contributed isolation and enzymatic characterization of polysaccharide lyase and glycoside hydrolase belonging new families (PL20, GH128) <cite>Konno2009a</cite> <cite>Konno2009b</cite> <cite>Sakamoto2011</cite>. His research currently focuses on various carbohydrate-active enzymes acting on fungal cell walls, such as chitinases <cite>Konno2012</cite>, beta-1,3-glucanases <cite>Sakamoto2011</cite> and beta-1,6-glucanases <cite>Konno2011</cite>. Some of these enzymes are involved in fungal morphological changes.

----

<biblio>
#Konno2009a pmid=18978091
#Konno2009b pmid=19306878
#Sakamoto2011 pmid=21965406
#Konno2012 pmid=22656067
#Konno2011 pmid=21523473
</biblio>

[[Category:Contributors|Konno,Naotake]]

User:Naotake Konno

2014-08-07T04:55:43Z

Naotake Konno:

----

[[File:Konno.pdf|200px|right]]
Naotake Konno is an associate professor at Department of Applied Biological Chemistry, Utsunomiya University, Japan. He obtained Ph. D. from Graduate School of The University of Tokyo in 2009. He contributed isolation and enzymatic characterization of polysaccharide lyase and glycoside hydrolase belonging new families (PL20, GH128) <cite>Konno2009a</cite> <cite>Konno2009b</cite> <cite>Sakamoto2011</cite>. His research currently focuses on various carbohydrate-active enzymes acting on fungal cell walls, such as chitinases <cite>Konno2012</cite>, beta-1,3-glucanases <cite>Sakamoto2011</cite> and beta-1,6-glucanases <cite>Konno2011</cite>. Some of these enzymes are involved in fungal morphological changes.

----

<biblio>
#Konno2009a pmid=18978091
#Konno2009b pmid=19306878
#Sakamoto2011 pmid=21965406
#Konno2012 pmid=22656067
#Konno2011 pmid=21523473
</biblio>

[[Category:Contributors|Naotake,Konno]]

File:Konno.pdf

2014-08-07T04:52:23Z

Naotake Konno:

User:Naotake Konno

2014-08-07T04:36:06Z

Naotake Konno: Created page with " ---- right Naotake Konno is an associate professor at Department of Applied Biological Chemistry, Utsu..."

----

[[file:///Users/konno/Desktop/研究室紹介/phot_konno.pdf|200px|right]]
Naotake Konno is an associate professor at Department of Applied Biological Chemistry, Utsunomiya University, Japan. He obtained Ph. D. from Graduate School of The University of Tokyo in 2009. He contributed isolation and enzymatic characterization of polysaccharide lyase and glycoside hydrolase belonging new families (PL20, GH128) <cite>Konno2009a</cite> <cite>Konno2009b</cite> <cite>Sakamoto2011</cite>. His research currently focuses on various carbohydrate-active enzymes acting on fungal cell walls, such as chitinases <cite>Konno2012</cite>, beta-1,3-glucanases <cite>Sakamoto2011</cite> and beta-1,6-glucanases <cite>Konno2011</cite>. Some of these enzymes are involved in fungal morphological changes.

----

<biblio>
#Konno2009a pmid=18978091
#Konno2009b pmid=19306878
#Sakamoto2011 pmid=21965406
#Konno2012 pmid=22656067
#Konno2011 pmid=21523473
</biblio>

[[Category:Contributors|Naotake,Konno]]