10.1098/rstb.1981.0057
Crossref journal-article
The Royal Society
Philosophical Transactions of the Royal Society of London. B, Biological Sciences (175)
Abstract

Recent results from the crystallographic studies on glycogen phosphorylase b at 3 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 that 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.

Bibliography

Phosphorylase: control and activity. (1981). Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 293(1063), 23–41.

Authors 0

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References 9 Referenced 25
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Dates
Type When
Created 18 years, 8 months ago (Dec. 15, 2006, 1:43 p.m.)
Deposited 4 years, 6 months ago (Feb. 14, 2021, 6:17 p.m.)
Indexed 1 year, 10 months ago (Oct. 24, 2023, 2:37 a.m.)
Issued 44 years, 2 months ago (June 26, 1981)
Published 44 years, 2 months ago (June 26, 1981)
Published Online 28 years, 8 months ago (Jan. 1, 1997)
Published Print 44 years, 2 months ago (June 26, 1981)
Funders 0

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@article{1981, volume={293}, ISSN={2054-0280}, url={http://dx.doi.org/10.1098/rstb.1981.0057}, DOI={10.1098/rstb.1981.0057}, number={1063}, journal={Philosophical Transactions of the Royal Society of London. B, Biological Sciences}, publisher={The Royal Society}, year={1981}, month=jun, pages={23–41} }