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Interplay of catalytic subsite residues in the positioning of α-d-glucose 1-phosphate in sucrose phosphorylase
Kinetic and molecular docking studies were performed to characterize the binding of α-d-glucose 1-phosphate (αGlc 1-P) at the catalytic subsite of a family GH-13 sucrose phosphorylase (from L. mesenteroides) in wild-type and mutated form. The best-fit binding mode of αGlc 1-P dianion had the phospha...
Gorde:
| Argitaratua izan da: | Biochem Biophys Rep |
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| Egile Nagusiak: | , , , , |
| Formatua: | Artigo |
| Hizkuntza: | Inglês |
| Argitaratua: |
Elsevier
2015
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| Gaiak: | |
| Sarrera elektronikoa: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4554294/ https://ncbi.nlm.nih.gov/pubmed/26380381 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbrep.2015.04.001 |
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