The tyrosyl residues in creatine kinase. Modification by iodine.
The effect of the iodination of tyrosyl residues in creatine kinase from rabbit muscle has been investigated at alkaline pH after reversible masking of the reactive thiol groups. The conversion of 4-5 tyrosyl residues to monoiodotyrosines as measured by spectrotitration and by radioactive iodine labelling resulted in almost total loss of enzymic activity. The modified enzyme was unable to bind its nucleotide substrates but no significant conformational change was revealed by optical rotatory dispersion or Stokes radius measurements. However, change in the reactivity of some non-essential thiol groups, presumably those located near the active thiol groups, was observed.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D003402:Creatine Kinase / Q000032:analysis* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007457:Iodine Radioisotopes; D009132:Muscles / Q000201:enzymology; D009905:Optical Rotatory Dispersion; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits; D013056:Spectrophotometry, Ultraviolet; D014443:Tyrosine / Q000032:analysis; D014508:Urea
D000596:Amino Acids; D007457:Iodine Radioisotopes; D014443:Tyrosine; D014508:Urea; D003402:Creatine Kinase