Article
Active site lysine promotes catalytic function of pyridoxal 5'-phosphate in alpha-glucan phosphorylases.
The Journal of biological chemistry - 25 May 1991
Schinzel R
Abstract excerpt
Tight contact of pyridoxal 5'-phosphate to the substrate phosphate is considered to be a crucial requirement of the phosphorolytic cleavage of polysaccharides by glycogen phosphorylases. This study demonstrates an essential role of lysine 533, the only charged residue in hydrogen bond distance to the phosphate of pyridoxal 5'-phosphate in Escherichia coli maltodextrin phosphorylase. Substitution of Lys533 by Ser...
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