Sturdík E, Drobnica L
Chem Biol Interact. 1980 Apr;30(1):105-4. doi: 10.1016/0009-2797(80)90118-0.
The inhibition of glycolysis by 2,3-dinitrilo-1,4-dithia-9,10-antraquinone (DDA) in Ehrlich ascites carcinoma (EAC) cells as well as in the investigated respiratory and fermentative strains of yeasts was found to be the result of inactivation of thiol enzymes of this pathway. Increasing concentration of DDA caused, in EAC cells, marked inhibition of hexokinase (HK), phosphofructokinase (PFK) and practically total inhibition of glyceraldehyde-3-phosphate dehydrogenase (GAPDH). These three enzymes, as well as alcohol dehydrogenase (ADH) were also inactivated by DDA in yeasts. DDA inhibited the biosynthetic processes as measured by following the rate of [14C]adenine and [14C)]valine incorporation into TCA-precipitable fractions proportionally to the degree of glucose consumption by EAC or the yeast cells.
研究发现,2,3 -二腈基-1,4 -二硫代-9,10 -蒽醌(DDA)对艾氏腹水癌细胞(EAC)以及所研究的酵母呼吸型和发酵型菌株的糖酵解具有抑制作用,这是该途径中硫醇酶失活的结果。在EAC细胞中,随着DDA浓度的增加,己糖激酶(HK)、磷酸果糖激酶(PFK)受到显著抑制,而甘油醛-3 -磷酸脱氢酶(GAPDH)几乎完全被抑制。在酵母中,这三种酶以及乙醇脱氢酶(ADH)也被DDA失活。通过追踪[¹⁴C]腺嘌呤和[¹⁴C]缬氨酸掺入三羧酸循环(TCA)沉淀部分的速率来衡量,DDA抑制生物合成过程,其抑制程度与EAC细胞或酵母细胞消耗葡萄糖的程度成正比。