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Glucose oxidase (GOX) catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone with the simultaneous reduction of enzyme-bound flavin. GOX exists as a homodimer, with each subunit binding one FAD molecule. Crystal structures show that FAD binds in a deep pocket of the enzyme near the dimer interface.
The interface between the two monomers of a single dimer of an ACAD contains the FAD binding sites and has extensive bonding interactions. In contrast, the interface between the two dimers has fewer interactions. There are a total of 4 active sites within the tetramer, each of which contains a single FAD molecule and an acyl-CoA substrate ...
About 5-10% of flavoproteins have a covalently linked FAD. [2] Based on the available structural data, FAD-binding sites can be divided into more than 200 different types. [3] 90 flavoproteins are encoded in the human genome; about 84% require FAD and around 16% require FMN, whereas 5 proteins require both. [4]
In this reaction, the substrate not only is oxidized but also loses a carbon dioxide molecule, and is attached to the CoA coenzyme.) glucose-6-phosphate dehydrogenase (involved in the pentose phosphate pathway, producing NADPH) glyceraldehyde-3-phosphate dehydrogenase (involved in glycolysis, uses NAD +) sorbitol dehydrogenase; TCA cycle examples:
FAD is the hydrogen acceptor, yielding FADH2. [7] 2. Enoyl-CoA hydrase catalyzes the addition of water across the newly formed double bond to make an alcohol. [5] [6] 3. 3-hydroxyacyl-CoA dehydrogenase oxidizes the alcohol group to a ketone. [5] NADH is produced from NAD+. [6] 4.
Glucose oxidase enzyme powder from Aspergillus niger. GOx is a dimeric protein, the 3D structure of which has been elucidated. The active site where glucose binds is in a deep pocket. The enzyme, like many proteins that act outside of cells, is covered with carbohydrate chains. GOx is a glucose oxidising enzyme with a molecular weight of 160 kDa.
Acetyl-CoA (acetyl coenzyme A) is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid metabolism. [2] Its main function is to deliver the acetyl group to the citric acid cycle (Krebs cycle) to be oxidized for energy production.
319945 Ensembl ENSG00000160688 ENSMUSG00000042642 UniProt Q8NFF5 Q8R123 RefSeq (mRNA) NM_001184891 NM_001184892 NM_025207 NM_201398 NM_177041 RefSeq (protein) NP_001171820 NP_001171821 NP_079483 NP_958800 NP_796015 NP_001349304 NP_001349305 Location (UCSC) Chr 1: 154.98 – 154.99 Mb Chr 3: 89.4 – 89.41 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Flavin adenine dinucleotide ...