Exploring glycolate oxidase (GOX) as an antiurolithic drug target: molecular modeling and in vitro inhibitor study

Int J Biol Macromol. 2011 Jul 1;49(1):62-70. doi: 10.1016/j.ijbiomac.2011.03.016. Epub 2011 Mar 30.


Glycolate oxidase (GOX) is one of the principal enzymes involved in the pathway of oxalate synthesis. It converts glycolate to glyoxylate by oxidation and then glyoxylate is finally converted to oxalate. Therapeutic intervention of GOX in this consequence thus found potential in the treatment of calcium oxalate urolithiasis. In present investigation, we explored GOX in search of potential leads from traditional resources. Molecular modeling of the identified leads, quercetin and kaempherol, was performed by employing Glide 5.5.211 (SchrodingerTM suite). In the absence of pure human glycolate oxidase (hGOX) preparation, in vitro experiments were performed on spinach glycolate oxidase (sGOX) as both enzymes possess 57% identity and 76% similarity along with several conserved active site residues in common. We aimed to identify a possible mechanism of action for the anti-GOX leads from Tribuls terrestris, which can be attributed to anti-urolithic drug development. This study found promising in development of future GOX inhibitory leads.

MeSH terms

  • Alcohol Oxidoreductases / antagonists & inhibitors*
  • Alcohol Oxidoreductases / chemistry
  • Alcohol Oxidoreductases / genetics
  • Amino Acid Sequence
  • Computational Biology
  • Drug Discovery / methods*
  • Flavonoids / pharmacology*
  • Humans
  • In Vitro Techniques
  • Kinetics
  • Models, Molecular*
  • Plant Extracts / pharmacology*
  • Sequence Alignment
  • Spinacia oleracea
  • Tribulus / chemistry*
  • Urolithiasis / drug therapy*


  • Flavonoids
  • Plant Extracts
  • Alcohol Oxidoreductases
  • glycollate oxidase