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. 1977 Nov;74(11):4762–4766. doi: 10.1073/pnas.74.11.4762

Complete amino acid sequence of rabbit muscle glycogen phosphorylase.

K Titani, A Koide, J Hermann, L H Ericsson, S Kumar, R D Wade, K A Walsh, H Neurath, E H Fischer
PMCID: PMC432035  PMID: 270711

Abstract

The sequence of the 841 amino acid residues in each subunit (molecular weight 97,412) of rabbit muscle glycogen phosphorylase b (1,4-alpha-D-glucan:orthophosphate alpha-glucosyltransferase; EC 2.4.1.1) has been determined. The general strategy was based on limited proteolysis of native phosphorylase b by subtilisin BPN', yielding two large segments (light and heavy) which were fragmented by cleavage at methyonyl-, asparaginyl-glycine, and aspartyl-proline bonds. Analysis of two cyanogen bromide fragments (CB14 and CB17) isolated from the intact molecule yielded the overlap between the light and heavy fragments and the remainder of the sequence. The residues involved in the covalent and allosteric control of the enzyme, and in the binding of the cofactor pyridoxal 5'-phosphate, were identified as serine-14, tyrosine-155, and lysine-679, respectively.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson R. A., Parrish R. F., Graves D. J. Chemistry of the adenosine monophosphate site of rabbit muscle glycogen phosphorylase. II. Properties of 8-(m-(m-gluorosulfonylbenzamido) benzylthio)adenine-modified phosphorylase. Biochemistry. 1973 May 8;12(10):1901–1906. doi: 10.1021/bi00734a010. [DOI] [PubMed] [Google Scholar]
  2. Avramovic-Zikic O., Smillie L. B., Madsen N. B. The sulfhydryl groups of muscle phosphorylase. IV. Reactivities as related to changes in protein structure. J Biol Chem. 1970 Apr 10;245(7):1558–1565. [PubMed] [Google Scholar]
  3. Battell M. L., Zarkadas C. G., Smillie L. B., Madsen N. B. The sulfhydryl groups of muscle phosphorylase. 3. Identification of cysteinyl peptides related to function. J Biol Chem. 1968 Dec 10;243(23):6202–6209. [PubMed] [Google Scholar]
  4. Bornstein P. Structure of alpha-1-CB8, a large cyanogen bromide produced fragment from the alpha-1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptides. Biochemistry. 1970 Jun 9;9(12):2408–2421. doi: 10.1021/bi00814a004. [DOI] [PubMed] [Google Scholar]
  5. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  6. Cohen P., Duewer T., Fischer E. H. Phosphorylase from dogfish skeletal muscle. Purification and a comparison of its physical properties to those of rabbit muscle phosphorylase. Biochemistry. 1971 Jul 6;10(14):2683–2694. doi: 10.1021/bi00790a005. [DOI] [PubMed] [Google Scholar]
  7. Edman P., Begg G. A protein sequenator. Eur J Biochem. 1967 Mar;1(1):80–91. doi: 10.1007/978-3-662-25813-2_14. [DOI] [PubMed] [Google Scholar]
  8. FISCHER E. H., KREBS E. G. The isolation and crystallization of rabbit skeletal muscle phosphorylase b. J Biol Chem. 1958 Mar;231(1):65–71. [PubMed] [Google Scholar]
  9. Fischer E. H., Pocker A., Saari J. C. The structure, function and control of glycogen phosphorylase. Essays Biochem. 1970;6:23–68. [PubMed] [Google Scholar]
  10. Fletterick R. J., Sygusch J., Semple H., Madsen N. B. Structure of glycogen phosphorylase a at 3.0 A resolution and its ligand binding sites at 6 A. J Biol Chem. 1976 Oct 10;251(19):6142–6146. [PubMed] [Google Scholar]
  11. Forrey A. W., Sevilla C. L., Saari J. C., Fischer E. H. Sequence of a segment of muscle glycogen phosphorylase containing the pyridoxal 5'-phosphate binding site. Biochemistry. 1971 Aug 3;10(16):3132–3140. doi: 10.1021/bi00792a023. [DOI] [PubMed] [Google Scholar]
  12. Fraser K. J., Pulsen K., Haber E. Specific cleavage between variable and constant domains of rabbit antibody light chains by dilute acid hydrolysis. Biochemistry. 1972 Dec 19;11(26):4974–4977. doi: 10.1021/bi00776a016. [DOI] [PubMed] [Google Scholar]
  13. Hermodson M. A., Ericsson L. H., Titani K., Neurath H., Walsh K. A. Application of sequenator analyses to the study of proteins. Biochemistry. 1972 Nov 21;11(24):4493–4502. doi: 10.1021/bi00774a011. [DOI] [PubMed] [Google Scholar]
  14. Houmard J., Drapeau G. R. Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds. Proc Natl Acad Sci U S A. 1972 Dec;69(12):3506–3509. doi: 10.1073/pnas.69.12.3506. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Johnson L. N., Madsen N. B., Mosley J., Wilson K. S. The crystal structure of phosphorylase beta at 6 A resolution. J Mol Biol. 1974 Dec 25;90(4):703–717. doi: 10.1016/0022-2836(74)90534-8. [DOI] [PubMed] [Google Scholar]
  16. NOLAN C., NOVOA W. B., KREBS E. G., FISCHER E. H. FURTHER STUDIES ON THE SITE PHOSPHORYLATED IN THE PHOSPHORYLASE B TO A REACTION. Biochemistry. 1964 Apr;3:542–551. doi: 10.1021/bi00892a013. [DOI] [PubMed] [Google Scholar]
  17. Omenn G. S., Fontana A., Anfinsen C. B. Modification of the single tryptophan residue of staphylococcal nuclease by a new mild oxidizing agent. J Biol Chem. 1970 Apr 25;245(8):1895–1902. [PubMed] [Google Scholar]
  18. Pisano J. J., Bronzert T. J. Analysis of amino acid phenylthiohydantoins by gas chromatography. J Biol Chem. 1969 Oct 25;244(20):5597–5607. [PubMed] [Google Scholar]
  19. Raibaud O., Goldberg M. E. Characterization of two complementary polypeptide chains obtained by proteolysis of rabbit muscle phosphorylase. Biochemistry. 1973 Dec 4;12(25):5154–5161. doi: 10.1021/bi00749a021. [DOI] [PubMed] [Google Scholar]
  20. Saari J. C., Fischer E. H. Cyanogen bromide peptides of rabbit muscle glycogen phosphorylase. Biochemistry. 1973 Dec 18;12(26):5225–5232. doi: 10.1021/bi00750a001. [DOI] [PubMed] [Google Scholar]
  21. Seery V. L., Fischer E. H., Teller D. C. A reinvestigation of the molecular weight of glycogen phosphorylase. Biochemistry. 1967 Oct;6(10):3315–3327. doi: 10.1021/bi00862a042. [DOI] [PubMed] [Google Scholar]
  22. Seery V. L., Fischer E. H., Teller D. C. Subunit structure of glycogen phosphorylase. Biochemistry. 1970 Sep 1;9(18):3591–3598. doi: 10.1021/bi00820a014. [DOI] [PubMed] [Google Scholar]
  23. Sevilla C. L., Fischer E. H. The purification and properties of rat muscle glycogen phosphorylase. Biochemistry. 1969 May;8(5):2161–2171. doi: 10.1021/bi00833a057. [DOI] [PubMed] [Google Scholar]
  24. Titani K., Cohen P., Walsh K. A., Neurath H. Amino-terminal sequence of rabbit muscle phosphorylase. FEBS Lett. 1975 Jul 15;55(1):120–123. doi: 10.1016/0014-5793(75)80974-4. [DOI] [PubMed] [Google Scholar]
  25. YAOI Y., TITANI K., NARITA K. N- AND C-TERMINAL RESIDUES IN BAKER'S YEAST CYTOCHROME C. J Biochem. 1964 Sep;56:222–229. doi: 10.1093/oxfordjournals.jbchem.a127984. [DOI] [PubMed] [Google Scholar]

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