CAZypedia - User contributions [en-ca]

User:Grete Raba

2023-08-25T23:20:10Z

Grete Raba:

[[Image:Grete.jpg|thumb|200px|right]]

I obtained my MSc in Chemistry and Biotechnology in 2016 at [https://taltech.ee/en/ Tallinn University of Technology], Estonia. I followed this with a PhD in the same department, under the supervision of Dr. [https://taltech.ee/en/contacts/division-food-and-biotechnology-0/kaarel-adamberg Kaarel Adamberg] and Dr. [https://www.gu.se/en/about/find-staff/liisaarike Liisa Arike], focusing on co-metabolism studies of dietary fibres and mucins by the gut microbiota <cite>Adamberg2020, Raba2021, Raba2023</cite>. At the start of 2023 I joined the lab of Dr. [https://www.cazypedia.org/index.php/User:Ana_Luis Ana S. Luis], part of the [http://www.medkem.gu.se/mucinbiology/ Mucin Biology Groups] of [https://www.gu.se/en Gothenburg University], Sweden. There, I am doing my post-doctoral research, studying the mechanisms of mucin degradation. More specifically, my focus is on the CAZymes involved in complex colonic mucin ''O''-glycan degradation by different gut commensal ''Bacteroides'' species.

----

<biblio>
#Adamberg2020 pmid=32117913
#Raba2021 pmid=33864456
#Raba2023 pmid=36695502

</biblio>


[[Category:Contributors|Raba,Grete]]

File:Grete.jpg

2023-08-25T22:53:37Z

Grete Raba:

Portrait of Grete Raba

Glycoside Hydrolase Family 143

2023-08-25T22:16:32Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH143'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining (inferred)
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH143.html
|}
</div>


== Substrate specificities ==
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 ==
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 ==
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 ==
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 ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH143]]

Glycoside Hydrolase Family 143

2023-08-25T22:15:12Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH143'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining (inferred)
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH143.html
|}
</div>


== Substrate specificities ==
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 ==
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 ==
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 ==
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 ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH143]]

Glycoside Hydrolase Family 142

2023-08-25T22:12:01Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH142'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|not known
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH142.html
|}
</div>


== Substrate specificities ==
The glycoside hydrolases from GH family 142 have β-L-arabinofuranosidase ([{{EClink}}3.2.1.185 EC 3.2.1.185]) activity. The first characterized enzyme from GH142 was the C-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. BT1020 C-terminus hydrolyses the β-1,5 linkage between L-arabinofuranosidase and D-DHA at the non-reducing end of rhamnogalacturonan II (RG II) D chain found in pectin.

== Kinetics and Mechanism ==
The kinetics and mechanisms of GH142 family remain to be elucidated.

== Catalytic Residues ==
The β-L-arabinofuranosidase from BT1020 C-terminus contains canonical glycoside hydrolase catalytic apparatus comprising carboxylate residues <cite>Ndeh2017</cite>.

== Three-dimensional structures ==
The β-L-arabinofuranosidase from the C-terminus of BT1020 has a (α/α)6-barrel structure <cite>Ndeh2017</cite>.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH142]]

Glycoside Hydrolase Family 142

2023-08-25T22:11:36Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH142'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|unknown
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH142.html
|}
</div>


== Substrate specificities ==
The glycoside hydrolases from GH family 142 have β-L-arabinofuranosidase ([{{EClink}}3.2.1.185 EC 3.2.1.185]) activity. The first characterized enzyme from GH142 was the C-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. BT1020 C-terminus hydrolyses the β-1,5 linkage between L-arabinofuranosidase and D-DHA at the non-reducing end of rhamnogalacturonan II (RG II) D chain found in pectin.

== Kinetics and Mechanism ==
The kinetics and mechanisms of GH142 family remain to be elucidated.

== Catalytic Residues ==
The β-L-arabinofuranosidase from BT1020 C-terminus contains canonical glycoside hydrolase catalytic apparatus comprising carboxylate residues <cite>Ndeh2017</cite>.

== Three-dimensional structures ==
The β-L-arabinofuranosidase from the C-terminus of BT1020 has a (α/α)6-barrel structure <cite>Ndeh2017</cite>.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH142]]

Glycoside Hydrolase Family 143

2023-08-25T22:07:51Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<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>


== Substrate specificities ==
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 ==
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 ==
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 ==
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 ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH143]]

Glycoside Hydrolase Family 143

2023-08-25T21:51:15Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<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>


== Substrate specificities ==
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 ==
Content is to be added here.

== Catalytic Residues ==
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 ==
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 ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH143]]

Glycoside Hydrolase Family 142

2023-08-25T21:49:13Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH142'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH142.html
|}
</div>


== Substrate specificities ==
The glycoside hydrolases from GH family 142 have β-L-arabinofuranosidase ([{{EClink}}3.2.1.185 EC 3.2.1.185]) activity. The first characterized enzyme from GH142 was the C-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. BT1020 C-terminus hydrolyses the β-1,5 linkage between L-arabinofuranosidase and D-DHA at the non-reducing end of rhamnogalacturonan II (RG II) D chain found in pectin.

== Kinetics and Mechanism ==
The kinetics and mechanisms of GH142 family remain to be elucidated.

== Catalytic Residues ==
The β-L-arabinofuranosidase from BT1020 C-terminus contains canonical glycoside hydrolase catalytic apparatus comprising carboxylate residues <cite>Ndeh2017</cite>.

== Three-dimensional structures ==
The β-L-arabinofuranosidase from the C-terminus of BT1020 has a (α/α)6-barrel structure <cite>Ndeh2017</cite>.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH142]]

Glycoside Hydrolase Family 142

2023-08-25T20:34:25Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH142'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH142.html
|}
</div>


== Substrate specificities ==
The glycoside hydrolases from GH family 142 have β-L-arabinofuranosidase ([{{EClink}}3.2.1.185 EC 3.2.1.185]) activity. The first characterized enzyme from GH142 was the C-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. BT1020 hydrolyses the β-1,5 linkage between L-arabinofuranosidase and D-DHA in the terminal region of rhamnogalacturonan II (RG II) D chain found in pectin.

== Kinetics and Mechanism ==
The kinetics and mechanisms of GH142 family remain to be elucidated.

== Catalytic Residues ==
The β-L-arabinofuranosidase from BT1020 C-terminus contains canonical glycoside hydrolase catalytic apparatus comprising carboxylate residues <cite>Ndeh2017</cite>.

== Three-dimensional structures ==
The β-L-arabinofuranosidase from the C-terminus of BT1020 has a (α/α)6-barrel structure <cite>Ndeh2017</cite>.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH142]]

Glycoside Hydrolase Family 143

2023-08-25T20:34:14Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<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>


== Substrate specificities ==
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 ==
Content is to be added here.

== Catalytic Residues ==
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 ==
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: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH143]]

Glycoside Hydrolase Family 143

2023-08-25T20:19:31Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<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>


== 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.

== Kinetics and Mechanism ==
Content is to be added here.

== Catalytic Residues ==
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 ==
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: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH143]]

Glycoside Hydrolase Family 142

2023-08-25T19:43:56Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH142'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH142.html
|}
</div>


== Substrate specificities ==
The glycoside hydrolases from GH family 142 have β-L-arabinofuranosidase (EC 3.2.1.185) activity. The first characterized enzyme from GH142 was the C-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. BT1020 hydrolyses the β-1,5 linkage between L-arabinofuranosidase and D-DHA in the terminal region of rhamnogalacturonan II (RG II) D chain found in pectin.

== Kinetics and Mechanism ==
The kinetics and mechanisms of GH142 family remain to be elucidated.

== Catalytic Residues ==
The β-L-arabinofuranosidase from BT1020 C-terminus contains canonical glycoside hydrolase catalytic apparatus comprising carboxylate residues <cite>Ndeh2017</cite>.

== Three-dimensional structures ==
The β-L-arabinofuranosidase from the C-terminus of BT1020 has a (α/α)6-barrel structure <cite>Ndeh2017</cite>.

== Family Firsts ==
;First stereochemistry determination: Not yet identified.
;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.
;First general acid/base residue identification: Not yet identified.
;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>.

== References ==
<biblio>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH142]]

Glycoside Hydrolase Family 142

2023-08-25T19:37:37Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH142'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH142.html
|}
</div>


== Substrate specificities ==
The glycoside hydrolases from GH family 142 have β-L-arabinofuranosidase (EC 3.2.1.185) activity. The first characterized enzyme from GH142 was the C-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <ref>Ndeh2017</ref>. BT1020 hydrolyses the β-1,5 linkage between L-arabinofuranosidase and D-DHA in the terminal region of rhamnogalacturonan II (RG II) D chain found in pectin.

== Kinetics and Mechanism ==
The kinetics and mechanisms of GH142 family remain to be elucidated.

== Catalytic Residues ==
The β-L-arabinofuranosidase from BT1020 C-terminus contains canonical glycoside hydrolase catalytic apparatus comprising carboxylate residues<ref>Ndeh2017</ref>.

== 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>
#Ndeh2017 pmid=28329766
</biblio>

[[Category:Glycoside Hydrolase Families|GH142]]

Glycoside Hydrolase Family 142

2023-08-25T19:19:23Z

Grete Raba:

Glycoside Hydrolase Family 142

2023-08-25T19:16:42Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH142'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH142.html
|}
</div>


== 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>
#Ndeh2017(pmid=28329766).

#Ndeh2017 Ndeh, D., Rogowski, A., Cartmell, A., Luis, A. S., Baslé, A., Gray, J., Venditto, I., Briggs, J., Zhang, X., Labourel, A., Terrapon, N., Buffetto, F., Nepogodiev, S., Xiao, Y., Field, R. A., Zhu, Y., O'Neill, M. A., Urbanowiczm B. R., York, W. S., Davies, G. J., Abbott, D. W., Ralet, M., Martens, E. C., Henrissat, B., Gilbert, H. J. (2017) Complex pectin metabolism by gut bacteria reveals novel catalytic functions. ''Nature'', vol. 544, no. 7648, pp. 65-70. (pmid=28329766).

#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|GH142]]

Glycoside Hydrolase Family 142

2023-08-25T19:15:48Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH142'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH142.html
|}
</div>


== 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>
#Ndeh2017 Ndeh, D., Rogowski, A., Cartmell, A., Luis, A. S., Baslé, A., Gray, J., Venditto, I., Briggs, J., Zhang, X., Labourel, A., Terrapon, N., Buffetto, F., Nepogodiev, S., Xiao, Y., Field, R. A., Zhu, Y., O'Neill, M. A., Urbanowiczm B. R., York, W. S., Davies, G. J., Abbott, D. W., Ralet, M., Martens, E. C., Henrissat, B., Gilbert, H. J. (2017) Complex pectin metabolism by gut bacteria reveals novel catalytic functions. ''Nature'', vol. 544, no. 7648, pp. 65-70. (pmid=28329766).

#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|GH142]]

Glycoside Hydrolase Family 142

2023-08-25T19:13:00Z

Grete Raba:

{{UnderConstruction}}
* [[Author]]: [[User:Grete Raba|Grete Raba]]
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH142'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH142.html
|}
</div>


== 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>
#Ndeh2017 Ndeh, D., Rogowski, A., Cartmell, A., Luis, A. S., Baslé, A., Gray, J., Venditto, I., Briggs, J., Zhang, X., Labourel, A., Terrapon, N., Buffetto, F., Nepogodiev, S., Xiao, Y., Field, R. A., Zhu, Y., O'Neill, M. A., Urbanowiczm B. R., York, W. S., Davies, G. J., Abbott, D. W., Ralet, M., Martens, E. C., Henrissat, B., Gilbert, H. J. (2017) Complex pectin metabolism by gut bacteria reveals novel catalytic functions. ''Nature'', vol. 544, no. 7648, pp. 65-70. [https://doi:10.1038/nature21725].

#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|GH142]]