Enzymes
| UniProtKB help_outline | 4,580 proteins |
| Enzyme class help_outline |
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- Name help_outline (S)-3-hydroxybutanoate Identifier CHEBI:11047 Charge -1 Formula C4H7O3 InChIKeyhelp_outline WHBMMWSBFZVSSR-VKHMYHEASA-M SMILEShelp_outline C[C@H](O)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 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 440 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (R)-2-hydroxyglutarate Identifier CHEBI:15801 Charge -2 Formula C5H6O5 InChIKeyhelp_outline HWXBTNAVRSUOJR-GSVOUGTGSA-L SMILEShelp_outline O[C@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetoacetate Identifier CHEBI:13705 (CAS: 141-81-1) help_outline Charge -1 Formula C4H5O3 InChIKeyhelp_outline WDJHALXBUFZDSR-UHFFFAOYSA-M SMILEShelp_outline CC(=O)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 23 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:23048 | RHEA:23049 | RHEA:23050 | RHEA:23051 | |
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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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Kinetic characterization of human hydroxyacid-oxoacid transhydrogenase: relevance to D-2-hydroxyglutaric and gamma-hydroxybutyric acidurias.
Struys E.A., Verhoeven N.M., Ten Brink H.J., Wickenhagen W.V., Gibson K.M., Jakobs C.
We investigated the presence of hydroxyacid-oxoacid transhydrogenase (HOT), which catalyses the cofactor-independent conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG), in human liver extracts employing ... >> More
We investigated the presence of hydroxyacid-oxoacid transhydrogenase (HOT), which catalyses the cofactor-independent conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG), in human liver extracts employing [2H6]GHB and 2-KG as substrates. We measured incorporation of 2H in D-[2H]2-HG using GC-MS analyses, providing evidence for HOT activity in humans. Kinetic characterization of HOT was undertaken in forward and reverse directions. We employed [2H6]GHB and [2H4]2-KG as cosubstrates in order to develop a HOT activity assay in cultured human fibroblasts derived from patients with D-2-hydroxyglutaric aciduria. HOT activity was quantified in this system by the measurement of D-[2H5]2-HG production. Fibroblasts derived from patients with D-2-hydroxyglutaric aciduria showed normal HOT activities. Our results provide the first demonstration and preliminary kinetic characterization of HOT activity in human tissues. << Less
J. Inherit. Metab. Dis. 28:921-930(2005) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Isolation and characterization of a hydroxyacid-oxoacid transhydrogenase from rat kidney mitochondria.
Kaufman E.E., Nelson T., Fales H.M., Levin D.M.
A transhydrogenase that catalyzes the oxoacid-dependent oxidation of specific hydroxyacids has been found in rat kidney, liver, and brain. The hydroxyacids that have been found to be substrates for this enzyme are gamma-hydroxybutyrate, D-alpha-hydroxyglutarate, and L-beta-hydroxybutyrate. The oxo ... >> More
A transhydrogenase that catalyzes the oxoacid-dependent oxidation of specific hydroxyacids has been found in rat kidney, liver, and brain. The hydroxyacids that have been found to be substrates for this enzyme are gamma-hydroxybutyrate, D-alpha-hydroxyglutarate, and L-beta-hydroxybutyrate. The oxoacids that are the best substrates for this enzyme are alpha-ketoglutarate and succinic semialdehyde; alpha-ketoadipate and oxalacetate are also substrates. This enzyme is located in the mitochondrial fraction of the cell and is not dependent on added NAD+ or NADP+. << Less
J. Biol. Chem. 263:16872-16879(1988) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.