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The study presents the first spectroscopic evidence of the formation of an intermediate with absorbance features resembling those of a flavosemiquinone in the oxidative half-reaction of glycolate oxidase.
These inhibitions suggest that glycolate binds to the active site of the reduced enzyme, and that DCIP (show SAMHD1 Proteins) also has affinity for the oxidized enzyme.
Active site and loop 4 movements within human glycolate oxidase.
This gene is one of three related genes that have 2-hydroxyacid oxidase activity yet differ in encoded protein amino acid sequence, tissue expression and substrate preference. Subcellular location of the encoded protein is the peroxisome. Specifically, this gene is expressed primarily in liver and pancreas and the encoded protein is most active on glycolate, a two-carbon substrate. The protein is also active on 2-hydroxy fatty acids. The transcript detected at high levels in pancreas may represent an alternatively spliced form or the use of a multiple near-consensus upstream polyadenylation site.
hydroxyacid oxidase 1
, Hydroxyacid oxidase 1
, hydroxyacid oxidase (glycolate oxidase) 1
, (S)-2-hydroxy-acid oxidase
, glycolate oxidase
, hydroxyacid oxidase 1, liver
, glycolate oxidase 1