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  • Title: An anion binding site in the active centre of phospholipase C from Bacillus cereus.
    Author: Aalmo K, Hansen L, Hough E, Jynge K, Krane J, Little C, Storm CB.
    Journal: Biochem Int; 1984 Jan; 8(1):27-33. PubMed ID: 6433934.
    Abstract:
    The bi-Zn2+-enzyme phospholipase C (Bacillus cereus) is readilly inhibited by univalent anions. N.m.r. studies on the 113Cd-substituted enzyme showed the presence of an inert and a perturbable metal, neither of which seemed affected by I-. X-ray crystallographic analysis showed the binding of one I- to the enzyme 4.8 A from the nearest metal (too far for a metal-halide bond). Phospholipase C contains an arginine residue apparently necessary for substrate binding and I- partially protected against inactivation by an arginine reagent. Thus an arginine residue may represent the binding site for univalent anions in the enzyme active centre.
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