Reaction participants Show >> << Hide
- Name help_outline 3-phenylpyruvate Identifier CHEBI:18005 (Beilstein: 3944391) help_outline Charge -1 Formula C9H7O3 InChIKeyhelp_outline BTNMPGBKDVTSJY-UHFFFAOYSA-M SMILEShelp_outline [O-]C(=O)C(=O)Cc1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-glutamine Identifier CHEBI:58359 Charge 0 Formula C5H10N2O3 InChIKeyhelp_outline ZDXPYRJPNDTMRX-VKHMYHEASA-N SMILEShelp_outline NC(=O)CC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 75 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-oxoglutaramate Identifier CHEBI:16769 (CAS: 18465-19-5) help_outline Charge -1 Formula C5H6NO4 InChIKeyhelp_outline COJBGNAUUSNXHX-UHFFFAOYSA-M SMILEShelp_outline NC(=O)CCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-phenylalanine Identifier CHEBI:58095 Charge 0 Formula C9H11NO2 InChIKeyhelp_outline COLNVLDHVKWLRT-QMMMGPOBSA-N SMILEShelp_outline [NH3+][C@@H](Cc1ccccc1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 74 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:17593 | RHEA:17594 | RHEA:17595 | RHEA:17596 | |
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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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Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K.
Han Q., Robinson H., Cai T., Tagle D.A., Li J.
Human kynurenine aminotransferase I (hKAT I) catalyzes the formation of kynurenic acid, a neuroactive compound. Here, we report three high-resolution crystal structures (1.50-1.55 A) of hKAT I that are in complex with glycerol and each of two inhibitors of hKAT I: indole-3-acetic acid (IAC) and Tr ... >> More
Human kynurenine aminotransferase I (hKAT I) catalyzes the formation of kynurenic acid, a neuroactive compound. Here, we report three high-resolution crystal structures (1.50-1.55 A) of hKAT I that are in complex with glycerol and each of two inhibitors of hKAT I: indole-3-acetic acid (IAC) and Tris. Because Tris is able to occupy the substrate binding position, we speculate that this may be the basis for hKAT I inhibition. Furthermore, the hKAT/IAC complex structure reveals that the binding moieties of the inhibitor are its indole ring and a carboxyl group. Six chemicals with both binding moieties were tested for their ability to inhibit hKAT I activity; 3-indolepropionic acid and DL-indole-3-lactic acid demonstrated the highest level of inhibition, and as they cannot be considered as substrates of the enzyme, these two inhibitors are promising candidates for future study. Perhaps even more significantly, we report the discovery of two different ligands located simultaneously in the hKAT I active center for the first time. << Less
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Purification of soluble and mitochondrial glutamine transaminase K from rat kidney. Use of a sensitive assay involving transamination between L-phenylalanine and alpha-keto-gamma-methiolbutyrate.
Cooper A.J.
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Isolation and properties of a new glutamine transaminase from rat kidney.
Cooper A.J., Meister A.