West T P
Experientia. 1985 Dec 15;41(12):1563-4. doi: 10.1007/BF01964808.
The maximal velocity of the reaction (Vmax) and the half-saturation constant (K0.5) values of the S. typhimurium cytosine deaminase were altered in the presence of its effectors, pyrophosphate and orotidine monophosphate. From the kinetics of orotidine monophosphate inhibition of cytosine deaminase, it was characterized as a mixed-type noncompetitive inhibitor.
在其效应物焦磷酸和乳清苷单磷酸存在的情况下,鼠伤寒沙门氏菌胞嘧啶脱氨酶的反应最大速度(Vmax)和半饱和常数(K0.5)值发生了改变。从乳清苷单磷酸对胞嘧啶脱氨酶的抑制动力学来看,它被表征为一种混合型非竞争性抑制剂。