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Literature summary for 3.2.1.81 extracted from
- Parallel substrate binding sites in a beta-agarase suggest a novel mode of action on double-helical agarose. [Erratum to document cited in CA141:067260] (2004), Structure, 12, 905.
No PubMed abstract available
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| inactive mutant A-E174S, in complex with agaro-octaose | Zobellia galactanivorans |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | inactive mutant A-E147S, crystallization data | Zobellia galactanivorans |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Zobellia galactanivorans | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Zobellia galactanivorans | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| neoagarooctaose + H2O = 2 neoagarotetraose | enzyme might be able to unwind the double-helical structure of substrate prior to the catalytic cleavage | Zobellia galactanivorans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| agarose + H2O | - |
Zobellia galactanivorans | ? | - |
? |  |
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