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  • Title: Involvement of a tyrosine residue in the ADP binding site of creatine kinase. A second-derivative UV-spectroscopy study.
    Author: Leydier C, Clottes E, Couthon F, Marcillat O, Vial C.
    Journal: Biochem Mol Biol Int; 1997 Apr; 41(4):777-84. PubMed ID: 9111938.
    Abstract:
    Second-derivative spectroscopy was used to determine the percentage of tyrosine residues that are exposed to solvent in rabbit MM-creatine kinase. Six residues, among the ten present per monomer, are solvent-exposed. The presence of creatine in the incubation medium does not modify this value. However, this number is decreased by one when the enzyme is incubated with saturating concentrations of MgADP. A dissociation constant for MgADP can be estimated and the obtained value (0.085 mM) is comparable to the Km for this substrate. Thus, a tyrosine residue is located near the MgADP binding site or is masked during protein conformational change induced by adenyl nucleotide binding.
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