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...

Celý popis

Uloženo v:
Podrobná bibliografie
Vydáno v:Biochem Biophys Rep
Hlavní autoři: Wildberger, Patricia, Aish, Gaia A., Jakeman, David L., Brecker, Lothar, Nidetzky, Bernd
Médium: Artigo
Jazyk:Inglês
Vydáno: Elsevier 2015
Témata:
Research Article
On-line přístup: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
Tagy: Přidat tag
Žádné tagy, Buďte první, kdo otaguje tento záznam!

Podobné jednotky