Studies on the Pyridoxal Phosphate Site in Glycogen Phosphorylase b
- 28 June 1976
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 65 (2) , 521-527
- https://doi.org/10.1111/j.1432-1033.1976.tb10369.x
Abstract
The adduct formed by reaction of pyridoxal phosphate with amines in aprotic solvents is considered a good model to simulate some properties of the pyridoxal phosphate site in [rabbit muscle] glycogen phosphorylase [.alpha.-1,4-glucan:orthophosphate glucosyltransferase EC 2.4.1.1]. The chemical structure of this adduct was not well established. An aldimine structure is supported by the infrared, electronic absorption and NMR spectra reported. Therefore, at neutral pH, the pyridoxal phosphate is bound to the glycogen phosphorylase through a Schiff base structure and embedded in a hydrophobic environment. The polarographic measurements reported could explain the inability of the pyridoxal phosphate to be reduced onto phosphorylase by NaBH4 at neutral pH.This publication has 25 references indexed in Scilit:
- Redox pattern for purine and 6-substituted purines in nonaqueous media. Free radical behaviorJournal of the American Chemical Society, 1974
- Intramolecular Proton Transfer in the Excited Singlet State of 3-Hydroxy-2-naphthoic AcidThe Journal of Chemical Physics, 1971
- The effect of solvent on the fluorescence of Schiff bases of pyridoxal 5′ phosphateBiochemical and Biophysical Research Communications, 1971
- The mode of binding of pyridoxal 5′-phosphate in glycogen phosphorylaseBiochemical and Biophysical Research Communications, 1970
- Pyridoxine and pyridoxal analogs. XIII. Nuclear magnetic resonance study of the condensation of polyfunctional amino acids with pyridoxalJournal of the American Chemical Society, 1970
- Catalytic Reactions Involving Azomethines. VII.1 Rates and Equilibria of Aldimine Formation with 3-Hydroxypyridine-4-aldehyde and AlanineJournal of the American Chemical Society, 1967
- Kinetics of the Stepwise Hydrolysis of Tetrahydroborate IonJournal of the American Chemical Society, 1965
- Proton Magnetic Resonance Spectra of Compounds in the Vitamin B6 GroupJournal of the American Chemical Society, 1963
- THE REACTION OF SODIUM BOROHYDRIDE WITH MUSCLE PHOSPHORYLASE1Journal of the American Chemical Society, 1958
- The isolation of pyridoxal-5-phosphate from crystalline muscle phosphorylaseBiochimica et Biophysica Acta, 1957