Reaction participants Show >> << Hide
- Name help_outline L-homoarginine Identifier CHEBI:143006 Charge 1 Formula C7H17N4O2 InChIKeyhelp_outline QUOGESRFPZDMMT-YFKPBYRVSA-O SMILEShelp_outline [O-]C([C@H](CCCCNC(N)=[NH2+])[NH3+])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-ornithine Identifier CHEBI:46911 Charge 1 Formula C5H13N2O2 InChIKeyhelp_outline AHLPHDHHMVZTML-BYPYZUCNSA-O SMILEShelp_outline [NH3+]CCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 58 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:70819 | RHEA:70820 | RHEA:70821 | RHEA:70822 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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The mitochondrial ornithine transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution of two human isoforms.
Fiermonte G., Dolce V., David L., Santorelli F.M., Dionisi-Vici C., Palmieri F., Walker J.E.
Two isoforms of the human ornithine carrier, ORC1 and ORC2, have been identified by overexpression of the proteins in bacteria and by study of the transport properties of the purified proteins reconstituted into liposomes. Both transport L-isomers of ornithine, lysine, arginine, and citrulline by ... >> More
Two isoforms of the human ornithine carrier, ORC1 and ORC2, have been identified by overexpression of the proteins in bacteria and by study of the transport properties of the purified proteins reconstituted into liposomes. Both transport L-isomers of ornithine, lysine, arginine, and citrulline by exchange and by unidirectional mechanisms, and they are inactivated by the same inhibitors. ORC2 has a broader specificity than ORC1, and L- and D-histidine, L-homoarginine, and D-isomers of ornithine, lysine, and ornithine are all substrates. Both proteins are expressed in a wide range of human tissues, but ORC1 is the predominant form. The highest levels of expression of both isoforms are in the liver. Five mutant forms of ORC1 associated with the human disease hyperornithinemia-hyperammonemia-homocitrullinuria were also made. The mutations abolish the transport properties of the protein. In patients with hyperornithinemia-hyperammonemia-homocitrullinuria, isoform ORC2 is unmodified, and its presence compensates partially for defective ORC1. << Less
J. Biol. Chem. 278:32778-32783(2003) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.