Pyridoxal phosphate-dependent conformational states of glycogen phosphorylase as probed by interconverting enzymes

Autor:	G W Tessmer, Donald J. Graves, T J Carty, J R Skuster, Gerald M. Carlson, R F Parrish
Rok vydání:	1975
Předmět:	chemistry.chemical_classification Purine nucleoside phosphorylase Cell Biology Biochemistry Serine chemistry.chemical_compound Glycogen phosphorylase (phosphorylase) phosphatase Enzyme chemistry Pyridoxal phosphate Phosphorylase kinase Molecular Biology Pyridoxal
Zdroj:	Journal of Biological Chemistry. 250:2254-2258
ISSN:	0021-9258
DOI:	10.1016/s0021-9258(19)41710-9
Popis:	The interaction between pyridoxal 5'-phosphate and the convertible serine of glycogen phosphorylase has been investigated by using: specific interconverting enzymes, phosphorylase kinase and phosphorylase phosphatase; effectors, glucose and glucose 6-phosphate; and a protein kinase and trypsin. Both phosphorylase kinase and phosphorylase phosphatase utilized the native protein while having little influence on the apoprotein. Removal of a peptide containing the critical serine residue gave phosphorylase b' from which the pyridoxal 5'-phosphate in phosphorylase has an important effect on enzymic interconversion.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::147faf491dc0ed48aa7a00e721803771 https://doi.org/10.1016/s0021-9258(19)41710-9 Zobrazit plný text záznamu