Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.2 Acting on the aldehyde or oxo group of donors
            1.2.3 With oxygen as acceptor
ID:1.2.3.5
Description:Glyoxylate oxidase.

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.2.3.5
BRENDA Enzyme Link: BRENDA 1.2.3.5
KEGG Enzyme Link: KEGG1.2.3.5
BioCyc Enzyme Link: BioCyc 1.2.3.5
ExPASy Enzyme Link: ExPASy1.2.3.5
EC2PDB Enzyme Link: EC2PDB 1.2.3.5
ExplorEnz Enzyme Link: ExplorEnz 1.2.3.5
PRIAM enzyme-specific profiles Link: PRIAM 1.2.3.5
IntEnz Enzyme Link: IntEnz 1.2.3.5
MEDLINE Enzyme Link: MEDLINE 1.2.3.5
MSA:

1.2.3.5;

Phylogenetic Tree:

1.2.3.5;

Uniprot:
M-CSA:
RHEA:14837 glyoxylate + H2O + O2 = H(+) + H2O2 + oxalate
RULE(radius=1) [*:1]=[CH;+0:2]-[*:3].[O;H0;+0:4]=[O;H0;+0:5].[OH2;+0:6]>>[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6].[OH;+0:4]-[OH;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design.Murray MS, Holmes RP, Lowther WT2008 Feb 2618215067
Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases.Jones JM, Morrell JC, Gould SJ2000 Apr 2810777549
Purification and characterization of recombinant human liver glycolate oxidase.Vignaud C, Pietrancosta N, Williams EL, Rumsby G, Lederer F2007 Sep 1517669354