Enzymes
| UniProtKB help_outline | 7 proteins |
Reaction participants Show >> << Hide
- Name help_outline urate Identifier CHEBI:17775 (CAS: 69-93-2) help_outline Charge 0 Formula C5H4N4O3 InChIKeyhelp_outline LEHOTFFKMJEONL-UHFFFAOYSA-N SMILEShelp_outline O=c1[nH]c2[nH]c(=O)[nH]c(=O)c2[nH]1 2D coordinates Mol file for the small molecule Search links Involved in 21 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-oxoglutarate Identifier CHEBI:16810 (CAS: 64-15-3) help_outline Charge -2 Formula C5H4O5 InChIKeyhelp_outline KPGXRSRHYNQIFN-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 449 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:72403 | RHEA:72404 | RHEA:72405 | RHEA:72406 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Human organic anion transporter 3 (hOAT3) can operate as an exchanger and mediate secretory urate flux.
Bakhiya A., Bahn A., Burckhardt G., Wolff N.
<h4>Background/aims</h4>Renal secretion of organic anions is critically dependent on their basolateral uptake against the electrochemical gradient. Due to their localization, two transporters are likely involved, namely OAT1 and OAT3. While OAT1 as an exchanger clearly operates in the secretory di ... >> More
<h4>Background/aims</h4>Renal secretion of organic anions is critically dependent on their basolateral uptake against the electrochemical gradient. Due to their localization, two transporters are likely involved, namely OAT1 and OAT3. While OAT1 as an exchanger clearly operates in the secretory direction, OAT3 in its previously supposed mode as a uniporter should move anionic substrates from cell to blood. It would thus dissipate gradients established by OAT1 of common OAT1/OAT3 substrates. In the present study we therefore reinvestigated the driving forces of human OAT3.<h4>Methods</h4>The human OAT3 obtained Xenopus laevis oocyte expression system, hOAT3-mediated transport of estrone sulfate (ES) and dicarboxylates was assayed for cis-inhibition and/or trans-stimulation in both the uptake and efflux direction.<h4>Results</h4>hOAT3-mediated efflux of glutarate (GA), can be significantly trans-stimulated by a variety of ions with high cis-inhibitory potency, including GA (282%), alpha-ketoglutarate (476%), p-aminohippurate (179%), and, most notably, urate (167%). Urate cis-inhibited ES uptake with an IC(50) close to normal serum urate concentrations.<h4>Conclusion</h4>These data indicate that OAT3 does not represent a uniporter but operates as an organic ion%dicarboxylate exchanger similar to OAT1, and may mediate renal urate secretion. << Less
Cell. Physiol. Biochem. 13:249-256(2003) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.