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Difference between revisions of "Glycoside Hydrolase Family 143"
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== Substrate specificities == | == 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 == | == Kinetics and Mechanism == | ||
Revision as of 12:34, 25 August 2023
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| Glycoside Hydrolase Family GH143 | |
| Clan | GH-x |
| Mechanism | retaining/inverting |
| Active site residues | known/not 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
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 [1].
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 [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 |