Asymmetry of subunits of aspartate aminotransferase in solution
DOI:
https://doi.org/10.7124/bc.000209Abstract
The apparent pK of enzyme-bound pyridoxal-5'-phosphate of subunits determined by circular dichroismic pH titralion of the pyridoxal form of aspartate aminotransferase (EC 2.6.1.1) amounts to pK1' = 5.55 ± 0.2, pK2' = 6.87 ± 0.14.References
Schlegel H, Christen P. The apo-holo hybrid of cytosolic aspartate aminotransferase, preparation and studies on subunit interactions. Biochem Biophys Res Commun. 1974;61(1):117-23.
Boettcher B, Martinez-Carrion M. Itemizing enzyme ligand interactions in native and and half-active hybrid aspartate transaminase to probe site-site relationships. Biochemistry. 1976;15(25):5657-64.
Arrio-Dupont M, Vergé D. Binding of substrates to aspartate aminotransferase. Evidence for a dissymmetrical binding. Eur J Biochem. 1982;125(1):183-7.
Kochkina VM, Kuznetsov DA. Catalytic properties of aspartate aminotransferase. Biokhimiia. 1986;51(6):921-5.
Jenkins WT, Yphantis DA, Sizer IW. Glutamic aspartic transaminase. I. Assay, purification, and general properties. J Biol Chem. 1959;234(1):51-7.
Salerno C., Giartosio A., Fasella P. Transaminases in vitamin B6 pyridoxal phosphate . Ed. D. Dolphin. New York : Wiley and Sons. 1986:117-168.
Verge D, Tenu JP, Arrio-Dupont M. Inorganic phosphate binding to apoaspartate aminotransferase. FEBS Lett. 1979;100(2):265-8.
