Glycolate Oxidases family
Contact author:Last update: 2021-12-02 (Bruno Savelli)
Glycolate Oxidases family (GOX)
Description
Glycolate oxidase belongs to a large group of oxidoreductases that act on alpha-hydroxy acids and which are FMN-containing flavoproteins [PUBMED:2324094, PUBMED:2271624, PUBMED:1939137].
Proteins belonging to this superfamily are structurally related and are the following: Lactate dehydrogenase (EC), which consists of a dehydrogenase domain and a haem-binding domain called cytochrome b2 and which catalyses the conversion of lactate into pyruvate. Glycolate oxidase (EC) ((S)-2-hydroxy-acid oxidase), a peroxisomal enzyme that catalyses the conversion of glycolate and oxygen to glyoxylate and hydrogen peroxide. Long chain alpha-hydroxy acid oxidase from rat (EC), a peroxisomal enzyme. Lactate 2-monooxygenase (EC) (lactate oxidase) from Mycobacterium smegmatis, which catalyses the conversion of lactate and oxygen to acetate, carbon dioxide and water. (S)-mandelate dehydrogenase from Pseudomonas putida (gene mdlB), which catalyses the reduction of (S)-mandelate to benzoylformate.
Literature
Davis A, Abbriano R, Smith SR, Hildebrand M. Clarification of Photorespiratory Processes and the Role of Malic Enzyme in Diatoms. Protist. 2017 Feb;168(1):134-153. PMID: 28104538.
Schmitz J, Srikanth NV, Hüdig M, Poschmann G, Lercher MJ, Maurino VG. The ancestors of diatoms evolved a unique mitochondrial dehydrogenase to oxidize photorespiratory glycolate. Photosynth Res. 2017 May;132(2):183-196. PMID: 28247236.
Hagemann M, Kern R, Maurino VG, Hanson DT, Weber AP, Sage RF, Bauwe H. Evolution of photorespiration from cyanobacteria to land plants, considering protein phylogenies and acquisition of carbon concentrating mechanisms. J Exp Bot. 2016 May;67(10):2963-76. PMID:26931168