Janse van Rensburg L, Schabort J C
Int J Biochem. 1984;16(5):547-51. doi: 10.1016/0020-711x(84)90173-3.
Initial velocity kinetic studies were undertaken and certain kinetic parameters ( KmSSO2 -3 = 3.1 X 10(-3) M and Vmax = 153.85 U/ml/min.) were determined and the mechanism identified as a ping-pong (double displacement) mechanism. Competitive inhibition of rhodanese by both substrates, viz. thiosulphate and cyanide, provides additional evidence of Ping-Pong Bi-Bi mechanism for this transferase.
进行了初始速度动力学研究,确定了某些动力学参数(KmSSO2 -3 = 3.1×10⁻³ M,Vmax = 153.85 U/ml/min),并确定该机制为乒乓(双置换)机制。两种底物,即硫代硫酸盐和氰化物对硫氰酸酶的竞争性抑制,为该转移酶的乒乓双底物机制提供了额外证据。