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Literature summary for 3.2.1.171 extracted from
- Mode of action of RG-hydrolase and RG-lyase toward rhamnogalacturonan oligomers. Characterization of degradation products using RG-rhamnohydrolase and RG-galacturonohydrolase (1998), Carbohydr. Res., 311, 155-164.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus aculeatus | Q00001 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| rhamnogalacturonan I + H2O | the enzyme is able to cleave rhamnogalacturonan oligomers which contain 5 rhamnose units or more (i.e. degree of polymerization 9) with a rhamnose unit at both nonreducing and reducing end. Its preferential cleavage site is at four units from the first nonreducing rhamnose. In hairy regions of pectin the rhamnogalacturonan stretches have to be at least 13 residues long for rhamnogalacturonan hydrolase to produce one tetramer | Aspergillus aculeatus | rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RG-hydrolase | - |
Aspergillus aculeatus |
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Release 2023.1 (January 2023)
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