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Literature summary for 3.2.1.131 extracted from
- Structural and functional characterization of a novel family GH115 4-O-methyl-alpha-glucuronidase with specificity for decorated Arabinogalactans (2015), J. Mol. Biol., 427, 3935-3946 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacteroides thetaiotaomicron | Q8A3J6 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme hydrolyzes terminal 4-O-methyl-glucuronic acid residues from decorated arabinogalactan isolated from acacia tree | Bacteroides thetaiotaomicron | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BtGH115A | - |
Bacteroides thetaiotaomicron |
| GH115 4-O-methyl-alpha-glucuronidase | - |
Bacteroides thetaiotaomicron |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | BtGH115A alpha-glucuronidase activity is necessary for the sequential digestion of branched galactans from acacia gum by a galactan-beta-1,3-galactosidase from family GH43. While Bacteroides thetaiotaomicron grows on larch wood arabinogalactan, the bacterium is not able to metabolize acacia gum arabinogalactan, suggesting that BtGH115A is involved in degradation of arabinogalactan fragments liberated by other microbial species in the gastrointestinal tract | Bacteroides thetaiotaomicron |
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