Abstract
Pyridoxal 5’-phosphate (PLP) is an essential constituent of glycogen phosphorylase (Baranowski et al., 1957). Removal of this cofactor from the enzyme, even under very mild, fully reversible conditions, results in an apoenzyme devoid of catalytic activity (Shaltiel et al., 1966; Hedrick et al., 1966). Furthermore, several properties of the PLP site suggest that the cofactor plays a key role in the enzyme by either participating directly in catalysis or by being involved in the transfer of a regulatory signal to or from the enzyme (cf. Shaltiel et al., 1972) .
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Veinberg, S., Steinberg, I.Z., Shaltiel, S. (1976). Excited-State vs Ground-State Structure of the Pyridoxal 5’-Phosphate Site in Glycogen Phosphorylase b . In: Shaltiel, S. (eds) Metabolic Interconversion of Enzymes 1975. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-66461-8_6
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DOI: https://doi.org/10.1007/978-3-642-66461-8_6
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