Lobb R R, Stokes A M, Hill H A, Riordan J F
Eur J Biochem. 1976 Nov 15;70(2):517-22. doi: 10.1111/j.1432-1033.1976.tb11043.x.
Rabbit muscle aldolase is irreversibly modified by the arginine-selective alpha-dicarbonyl, phenylglyoxal, loss of activity correlating with the unique modifications of one arginine residue per subunit, as determined by amino acid analysis, and (7-14C)phenylglyoxal incorporation. The affinity of the modified enzyme for dihydroxyacetone phosphate is significantly reduced while substantial protection against inactivation is afforded by fructose 1,6-disphosphate, dihydroxyacetone phosphate or phosphate ion. The nature of the substrate C-1 phosphate binding site in this enzyme is discussed in the light of these and other results.
兔肌肉醛缩酶可被精氨酸选择性α-二羰基化合物苯乙二醛不可逆修饰，活性丧失与每个亚基一个精氨酸残基的独特修饰相关，这是通过氨基酸分析和（7-¹⁴C）苯乙二醛掺入确定的。修饰后的酶对磷酸二羟丙酮的亲和力显著降低，而1,6-二磷酸果糖、磷酸二羟丙酮或磷酸离子对失活有显著保护作用。根据这些及其他结果讨论了该酶中底物C-1磷酸结合位点的性质。
