Human muscle glycogen synthase cDNA sequence: a negatively charged protein with an asymmetric charge distribution.
- 1 March 1989
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 86 (5) , 1443-1447
- https://doi.org/10.1073/pnas.86.5.1443
Abstract
The cDNA for human muscle glycogen synthase encodes a protein of 737 amino acids. The primary structure of glycogen synthase is not related either to bacterial glycogen synthase or to any glycogen phosphorylase. All nine of the serines that are phosphorylated in the rabbit muscle enzyme in vivo are conserved in the human muscle sequence. The amino- and carboxyl-terminal fragments, which contain all the phosphorylation sites, are very negatively charged. Overall the unphosphorylated protein has a charge of -13, while the fully phosphorylated inactive protein has a net charge of -31. The importance of the asymmetrical charge distribution is discussed.This publication has 32 references indexed in Scilit:
- Structural changes in glycogen phosphorylase induced by phosphorylationNature, 1988
- Analysis of the in vivo phosphorylation state of rabbit skeletal muscle glycogen synthase by fast‐atom‐bombardment mass spectrometryEuropean Journal of Biochemistry, 1988
- Regional distant sequence homology between amylases, α‐glucosidases and transglucanosylasesFEBS Letters, 1988
- Identification of the 38‐kDa subunit of rabbit skeletal muscle glycogen synthase as glycogeninEuropean Journal of Biochemistry, 1987
- Complete cloning of the duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individualsCell, 1987
- Complete cDNA sequence for rabbit muscle glycogen phosphorylaseFEBS Letters, 1986
- A novel glycosyl-amino acid linkage: Rabbit-muscle glycogen is covalently linked to a protein via tyrosineBiochemical and Biophysical Research Communications, 1985
- BACTERIAL GLYCOGEN SYNTHESIS AND ITS REGULATIONAnnual Review of Microbiology, 1984
- Structure of maltoheptaose by difference Fourier methods and a model for glycogenJournal of Molecular Biology, 1982
- Kinetic mechanism of rabbit muscle glycogen synthase IBiochemistry, 1980