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Literature summary for 3.2.1.149 extracted from
- Toward a blueprint for beta -primeverosidase from tea leaves structure/function properties: Homology modeling study (2006), J. Theor. Comput. Chem., 5, 433-446.
No PubMed abstract available
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Camellia sinensis | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Camellia sinensis | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| a beta-primeveroside + H2O | the enzyme shows broad substrate specificity with respect to the disaccharide glycon moiety (subsite-2), Thr271 and Thr415 play important roles in subsite-2 of the enzyme | Camellia sinensis | ? + primeverose | - |
? |  |
| additional information | does not act on 2-phenylethyl beta-D-glucopyranoside | Camellia sinensis | ? | - |
? | |
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Release 2023.1 (January 2023)
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