Details

Autor(en) / Beteiligte

• Jenkins, J A
• Johnson, L N
• Stuart, D I
• Stura, E A
• Wilson, K S
• Zanotti, G

Titel

Phosphorylase: control and activity

Ist Teil von

• Philosophical transactions of the Royal Society of London. Series B. Biological sciences, 1981-06, Vol.293 (1063), p.23

Ort / Verlag

England

Erscheinungsjahr

1981

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Recent results from the crystallographic studies on glycogen phosphorylase b at 2 A resolution are reviewed with special reference to other themes of the meeting. The structural similarity of the fold of 150 residues in phosphorylase to the observed in lactate dehydrogenase is discussed and the binding sites for NADH in phosphorylase are described. The binding of the potent inhibitor glucose-1,2-cyclic phosphate to phosphorylase b in the crystal has been studied at 3 A resolution. The results are compared with those previously obtained for glucose-1-phosphate and discussed with reference to proposals for a mechanism of catalysis that involves the essential cofactor pyridoxal phosphate.