Summary
The gene encoding E. coli maltodextrin phosphorylase has been cloned and overexpressed to 10–20mg/L levels in E. coli host cells deficient in wild type phosphorylase activity. Mutagenesis of Lys533 and Glu637 affect Km and kcat values to a different extent. The results suggest that Lys533 together wTtri pyridoxal phosphate are part of a proton transfer relay and Glu637 modifies phosphate binding in the ground and transition state.
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© 1987 Birkhäuser Verlag Basel
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Palm, D., Schinzel, R., Zeier, R., Klein, H. (1987). Site-Specific Mutations in E. coli Maltodextrin Phosphorylase With Differential Effects on Substrate Binding and Catalysis. In: Korpela, T.K., Christen, P. (eds) Biochemistry of Vitamin B6 . Birkhäuser Congress Reports. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-9308-4_15
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DOI: https://doi.org/10.1007/978-3-0348-9308-4_15
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