View the latest EBI news stories and important announcements...

Search The CSA
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1gox

E.C. name(S)-2-hydroxy-acid oxidase
SpeciesSpinacia oleracea (Spinach)
E.C. Number (IntEnz)
CSA Homologues of 1goxThere are 31 Homologs
CSA Entries With UniProtID P05414
CSA Entries With EC Number
PDBe Entry 1gox
PDBSum Entry 1gox
MACiE Entry 1gox

Literature Report

IntroductionGlycolate oxidase is a flavoenzyme, which contains a permanently bound FNN cofactor. It catalyses the oxidation of (S)-2-hydroxy-acid to 2-oxo acid. In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. Comparison of properties with the extensively studied L-lactate oxidase and the topography of the active site and the amino acids surrounding the prosthetic group FMN led to the proposal of a reaction mechanism.
MechansimThe reaction proceeds via a ping-pong mechanism and the reduction of FMN is found to be rate-limiting. In the first reductive step a proton is abstracted from the substance C2 carbon atom producing a carbanion. This carbanion can subsequently attach to a N5 atom of FMN, via formation of a covalent adduct, two electrons are then transferred to the isoalloxazine ring. The reduced FMN is reoxidised by oxygen to form hydrogen peroxide.

Catalytic Sites for 1gox

Literature References

Notes:Note in contrast to the previous entry I have not included Arg-275 or Tyr-24 as their functions are solely to bind the substrate so far as specified in the literature and hence are not catalytic residues. Lys-230 however has been included as it contributes towards the catalytic mechanism.
Macheroux P
Role of tyrosine 129 in the active site of spinach glycolate oxidase.
Eur J Biochem 1993 213 1047-1054
PubMed: 8504801
Lindqvist Y
The active site of spinach glycolate oxidase.
J Biol Chem 1989 264 3624-3628
PubMed: 2644287