Orthophosphate binding at the dimer interface of Corynebacterium callunae starch phosphorylase: mutational analysis of its role for activity and stability of the enzyme-Reference-Cited by-同舟云学术

Orthophosphate binding at the dimer interface of Corynebacterium callunae starch phosphorylase: mutational analysis of its role for activity and stability of the enzyme

Published:2010 Issue:1 Volume:11 Page:8
ISSN:1471-2091
Container-title:BMC Biochemistry
language:en
Short-container-title:BMC Biochemistry

Author:

Mueller Mario,Nidetzky Bernd

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Biochemistry

Reference19 articles.

1. An Evolving Hierarchical Family Classification for Glycosyltransferases

2. The role of pyridoxal 5'-phosphate in glycogen phosphorylase catalysis

3. Catalytic site of glycogen phosphorylase: structural changes during activation and mechanistic implications

4. Functions of the 5'-phosphoryl group of pyridoxal 5'-phosphate in phosphorylase: a study using pyridoxal-reconstituted enzyme as a model system

5. The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase

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