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Difference between revisions of "Glycoside Hydrolase Family 143"
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{{UnderConstruction}} | {{UnderConstruction}} | ||
| − | * [[Author]]: [[User: | + | * [[Author]]: [[User:Grete Raba|Grete Raba]] |
* [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]] | * [[Responsible Curator]]: [[User:Ana Luis|Ana Luis]] | ||
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|'''Mechanism''' | |'''Mechanism''' | ||
| − | |retaining | + | |retaining (inferred) |
|- | |- | ||
|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |known |
|- | |- | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
| Line 29: | Line 29: | ||
== Substrate specificities == | == 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 == | == 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 == | == 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 == | == 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 == | == Family Firsts == | ||
| − | ;First stereochemistry determination: | + | ;First stereochemistry determination: Not yet identified. |
| − | ;First catalytic nucleophile identification: | + | ;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. |
| − | ;First general acid/base residue identification: | + | ;First general acid/base residue identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. |
| − | ;First 3-D structure: | + | ;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. |
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #Ndeh2017 pmid=28329766 |
| − | |||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH143]] | [[Category:Glycoside Hydrolase Families|GH143]] | ||
Latest revision as of 14:16, 25 August 2023
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
| Glycoside Hydrolase Family GH143 | |
| Clan | GH-x |
| Mechanism | retaining (inferred) |
| Active site residues | known |
| CAZy DB link | |
| https://www.cazy.org/GH143.html | |
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 [1]. 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 [1]. 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 [1].
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 [1].
Family Firsts
- First stereochemistry determination
- Not yet identified.
- First catalytic nucleophile identification
- BT1020 from Bacteroides thetaiotaomicron [1].
- First general acid/base residue identification
- BT1020 from Bacteroides thetaiotaomicron [1].
- First 3-D structure
- BT1020 from Bacteroides thetaiotaomicron [1].
References
- Ndeh D, Rogowski A, Cartmell A, Luis AS, Baslé A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neil MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, and Gilbert HJ. (2017). Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature. 2017;544(7648):65-70. DOI:10.1038/nature21725 |