Enzymes
UniProtKB help_outline | 27,003 proteins |
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- Name help_outline a quinone Identifier CHEBI:132124 Charge 0 Formula C6O2R4 SMILEShelp_outline O=C1C(*)=C(*)C(=O)C(*)=C1* 2D coordinates Mol file for the small molecule Search links Involved in 127 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline sn-glycerol 3-phosphate Identifier CHEBI:57597 (Beilstein: 6115564) help_outline Charge -2 Formula C3H7O6P InChIKeyhelp_outline AWUCVROLDVIAJX-GSVOUGTGSA-L SMILEShelp_outline OC[C@@H](O)COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 52 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dihydroxyacetone phosphate Identifier CHEBI:57642 (Beilstein: 4428349) help_outline Charge -2 Formula C3H5O6P InChIKeyhelp_outline GNGACRATGGDKBX-UHFFFAOYSA-L SMILEShelp_outline C(CO)(COP([O-])(=O)[O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 41 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a quinol Identifier CHEBI:24646 Charge 0 Formula C6H2O2R4 SMILEShelp_outline OC1=C(*)C(*)=C(O)C(*)=C1* 2D coordinates Mol file for the small molecule Search links Involved in 238 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:18977 | RHEA:18978 | RHEA:18979 | RHEA:18980 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants.
Shen W., Wei Y., Dauk M., Zheng Z., Zou J.
We report molecular characterization of an Arabidopsis gene encoding a mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase (FAD-GPDH) that oxidizes glycerol-3-phosphate (G-3-P) to dihydroxyacetone phosphate. We demonstrate through in vitro targeting assays that the encoded gene product ... >> More
We report molecular characterization of an Arabidopsis gene encoding a mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase (FAD-GPDH) that oxidizes glycerol-3-phosphate (G-3-P) to dihydroxyacetone phosphate. We demonstrate through in vitro targeting assays that the encoded gene product can be imported into mitochondrial membrane systems. Enzyme activity of the protein was confirmed through heterologous expression in Escherichia coli. The Arabidopsis gene is expressed throughout plant development, but at the highest level during seed germination. We also show that expression of the Arabidopsis FAD-GPDH gene is coupled to oxygen consumption and affected by ABA and stress conditions. Together with an NAD(+)-dependent GPDH, this enzyme could form a G-3-P shuttle, as previously established in other eukaryotic organisms, and links cytosolic G-3-P metabolism to carbon source utilization and energy metabolism in plants. << Less
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Steady-state kinetics of reduction of coenzyme Q analogs by glycerol-3-phosphate dehydrogenase in brown adipose tissue mitochondria.
Rauchova H., Fato R., Drahota Z., Lenaz G.
We have undertaken a study of the role of coenzyme Q (CoQ) in glycerol-3-phosphate oxidation in mitochondrial membranes from hamster brown adipose tissue, using either quinone homologs, as CoQ1 and CoQ2, or the analogs duroquinone and decylubiquinone as artificial electron acceptors. We have found ... >> More
We have undertaken a study of the role of coenzyme Q (CoQ) in glycerol-3-phosphate oxidation in mitochondrial membranes from hamster brown adipose tissue, using either quinone homologs, as CoQ1 and CoQ2, or the analogs duroquinone and decylubiquinone as artificial electron acceptors. We have found that the most suitable electron acceptor for glycerol-3-phosphate:CoQ reductase activity in situ in the mitochondrial membrane is the homolog CoQ1 yielding the highest rate of enzyme activity (225 +/-41 nmol x min(-1) x mg(-1) protein). With all acceptors tested the quinone reduction rates were completely insensitive to Complex III inhibitors, indicating that all acceptors were easily accessible to the quinone-binding site of the dehydrogenase preferentially with respect to the endogenous CoQ pool, in such a way that Complex III was kept in the oxidized state. We have also experimentally investigated the saturation kinetics of endogenous CoQ (1.35 nmol/mg protein of a mixture of 70% CoQ9 and 30% CoQ10) by stepwise pentane extraction of brown adipose tissue mitochondria and found a K(m) of the integrated activity of glycerol-3-phosphate cytochrome c reductase for endogenous CoQ of 0.22 nmol/mg protein, indicating that glycerol-3-phosphate-supported respiration is over 80% of V(max) with respect to the CoQ pool. A similar K(m) of 0.19 nmol CoQ/mg protein was found in glycerol-3-phosphate cytochrome c reductase in cockroach flight muscle mitochondria. << Less
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Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic alpha-helix.
Walz A.C., Demel R.A., de Kruijff B., Mutzel R.
sn-Glycerol-3-phosphate dehydrogenase (GlpD) from Escherichia coli is a peripheral membrane enzyme involved in respiratory electron transfer. For it to display its enzymic activity, binding to the inner membrane is required. The way the enzyme interacts with the membrane and how this controls acti ... >> More
sn-Glycerol-3-phosphate dehydrogenase (GlpD) from Escherichia coli is a peripheral membrane enzyme involved in respiratory electron transfer. For it to display its enzymic activity, binding to the inner membrane is required. The way the enzyme interacts with the membrane and how this controls activity has not been elucidated. In the present study we provide evidence for direct protein-lipid interaction. Using the monolayer technique, we observed insertion of GlpD into lipid monolayers with a clear preference for anionic phospholipids. GlpD variants with point mutations in their predicted amphipathic helices showed a decreased ability to penetrate anionic phospholipid monolayers. From these data we propose that membrane binding of GlpD occurs by insertion of an amphipathic helix into the acyl-chain region of lipids mediated by negatively charged phospholipids. << Less