The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes
The mechanism and the site of substrate (i.e., aglycone) recognition and specificity were investigated in maize β-glucosidase (Glu1) by x-ray crystallography by using crystals of a catalytically inactive mutant (Glu1E191D) in complex with the natural substrate 2-O-β-d-glucopyranosyl-4-hydroxy-7-meth...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
2000
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC17614/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11106394/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.97.25.13555 |
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