Sejlitz T, Neujahr H Y
Department of Biochemistry and Biotechnology, Royal Institute of Technology, Stockholm, Sweden.
J Protein Chem. 1991 Feb;10(1):43-8. doi: 10.1007/BF01024654.
Phenol hydroxylase was inactivated by the arginine reagents 2,3-butanedione, 1,2-cyclohexanedione, and phenylglyoxal. The cosubstrate NADPH, as well as NADPH+ and several analogues thereof, protected the enzyme against inactivation. Phenol did not protect the activity against any of the reagents used, nor did modification by 2,3-butanedione affect the binding of phenol. We propose the presence of arginyl residues in the binding sites for the adenosine phosphate part of NADPH.
苯酚羟化酶被精氨酸试剂2,3 - 丁二酮、1,2 - 环己二酮和苯乙二醛失活。共底物NADPH以及NADPH⁺及其几种类似物可保护该酶不被失活。苯酚不能保护该酶的活性免受所使用的任何一种试剂的影响，2,3 - 丁二酮的修饰也不影响苯酚的结合。我们推测在NADPH的磷酸腺苷部分的结合位点存在精氨酰残基。
