Glycolate oxidase: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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-<StructureSection load='2rdu' size='350' side='right' caption='Human glycolate oxidase 1 complex with glyoxylate and FMN (PDB entry [[2rdu]])' scene='48/486364/Cv/1'>
+<StructureSection load='' size='350' side='right' caption='Human glycolate oxidase 1 complex with glyoxylate and FMN (PDB entry [[2rdu]])' scene='48/486364/Cv/1'>
 == Function ==
-'''Glycolate oxidase''' (GOX) catalyzes the conversion of (S)-2-hydroxy acid and molecular oxygen to 2-oxo acid and hydrogen peroxide.  In higher plants, GOX catalyzes the oxidation of glycolate to glyoxylate.  GOX is part of the glyoxylate and dicarboxylate metabolism and uses FMN as a cofactor.  GOX catalyzes the first step in the utilization of glycolate as the sole source of carbon<ref>PMID:22286136</ref>.
+'''Glycolate oxidase''' (GOX) or '''hydroxyacid oxidase''' catalyzes the conversion of (S)-2-hydroxy acid and molecular oxygen to 2-oxo acid and hydrogen peroxide.  In higher plants, GOX catalyzes the oxidation of glycolate to glyoxylate.  GOX is part of the glyoxylate and dicarboxylate metabolism and uses FMN as a cofactor.  GOX catalyzes the first step in the utilization of glycolate as the sole source of carbon<ref>PMID:22286136</ref>.
 == Disease ==
 Mutations in GOX result in isolated asymptotic hyperoxaluria type I<ref>PMID:24996905</ref>.
 == Structural highlights ==
-The biological assembly of human glycolate oxidase 1 <scene name='48/486364/Cv/2'>homotetramer</scene>. GOX structure shows the typical β8/α8 fold of an α-hydroxy acid oxidase and its active site contains the cofactor FMN<ref>PMID:18215067</ref>.
+The biological assembly of human glycolate oxidase 1 <scene name='48/486364/Cv/7'>homotetramer</scene>. GOX structure shows the <scene name='48/486364/Cv/8'>typical β8/α8 fold</scene> ({{Template:ColorKey_Helix}},
-</StructureSection>
+{{Template:ColorKey_Strand}},
+{{Template:ColorKey_Loop}},
+{{Template:ColorKey_Turn}}
+) of an α-hydroxy acid oxidase and its <scene name='48/486364/Cv/9'>active site contains the cofactor FMN</scene><ref>PMID:18215067</ref>. Water molecules are shown as red spheres.
 ==3D structures of glycolate oxidase==
+[[Glycolate oxidase 3D structures]]
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+</StructureSection>
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*Glycolate oxidase
-**[[1gyl]] – sGOX – spinach<br />
-**[[2nzl]] – hGOX1 – human<br />
-**[[2yvs]] – GOX GLCE subunit – ''Thermus thermophilus''<br />
-**[[1tb3]] – rGOX3 – rat
-*Glycolate oxidase complex
-**[[1al8]], [[1al7]] – sGOX + inhibitor<br />
-**[[2rdu]] – hGOX1 + glyoxylate<br />
-**[[2rdw]] – hGOX1 + sulfate<br />
-**[[2w0u]], [[2rdt]] – hGOX1 + inhibitor<br />
-**[[3sgz]] – rGOX2 + inhibitor<br />
-**[[3giy]] – GOX1/(S)-mandelate dehydrogenase + MES – ''Pseudomonas putida''
-}}
 == References ==
 <references/>
 [[Category:Topic Page]]