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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.

Citation

C Leydier, E Clottes, F Couthon, O Marcillat, C Vial. Involvement of a tyrosine residue in the ADP binding site of creatine kinase. A second-derivative UV-spectroscopy study. Biochemistry and molecular biology international. 1997 Apr;41(4):777-84

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PMID: 9111938

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