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Literature summary for 4.2.2.23 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 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| rhamnogalacturonan I | RG-lyase is active toward oligomers that contain at least six GalA units, i.e. degree of polymerization 12 with a GalA at the nonreducing and a Rha at the reducing end. The preferential cleavage site is for the smaller oligomers four residues, and for the largest oligomer six residues from the reducing Rha. From the observed cleavage patterns it can be speculated that in hairy regions, the rhamnogalacturonan stretches have to be at least 16 residues long for the RG-lyase in order to produce one tetramer | Aspergillus aculeatus | rhamnogalacturonan I oligosaccharides with alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the nonreducing end | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RG-lyase | - |
Aspergillus aculeatus |
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Release 2023.1 (January 2023)
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