Enzymes
| UniProtKB help_outline | 902 proteins |
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- Name help_outline 4-methylsulfanyl-2-oxobutanoate Identifier CHEBI:16723 (Beilstein: 3662236) help_outline Charge -1 Formula C5H7O3S InChIKeyhelp_outline SXFSQZDSUWACKX-UHFFFAOYSA-M SMILEShelp_outline CSCCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 19 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-kynurenine Identifier CHEBI:57959 Charge 0 Formula C10H12N2O3 InChIKeyhelp_outline YGPSJZOEDVAXAB-QMMMGPOBSA-N SMILEShelp_outline Nc1ccccc1C(=O)C[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 34 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline kynurenate Identifier CHEBI:58454 Charge -1 Formula C10H6NO3 InChIKeyhelp_outline HCZHHEIFKROPDY-UHFFFAOYSA-M SMILEShelp_outline Oc1cc(nc2ccccc12)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 19 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-methionine Identifier CHEBI:57844 Charge 0 Formula C5H11NO2S InChIKeyhelp_outline FFEARJCKVFRZRR-BYPYZUCNSA-N SMILEShelp_outline CSCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 131 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:69096 | RHEA:69097 | RHEA:69098 | RHEA:69099 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II.
Han Q., Cai T., Tagle D.A., Robinson H., Li J.
KAT (kynurenine aminotransferase) II is a primary enzyme in the brain for catalysing the transamination of kynurenine to KYNA (kynurenic acid). KYNA is the only known endogenous antagonist of the N-methyl-D-aspartate receptor. The enzyme also catalyses the transamination of aminoadipate to alpha-o ... >> More
KAT (kynurenine aminotransferase) II is a primary enzyme in the brain for catalysing the transamination of kynurenine to KYNA (kynurenic acid). KYNA is the only known endogenous antagonist of the N-methyl-D-aspartate receptor. The enzyme also catalyses the transamination of aminoadipate to alpha-oxoadipate; therefore it was initially named AADAT (aminoadipate aminotransferase). As an endotoxin, aminoadipate influences various elements of glutamatergic neurotransmission and kills primary astrocytes in the brain. A number of studies dealing with the biochemical and functional characteristics of this enzyme exist in the literature, but a systematic assessment of KAT II addressing its substrate profile and kinetic properties has not been performed. The present study examines the biochemical and structural characterization of a human KAT II/AADAT. Substrate screening of human KAT II revealed that the enzyme has a very broad substrate specificity, is capable of catalysing the transamination of 16 out of 24 tested amino acids and could utilize all 16 tested alpha-oxo acids as amino-group acceptors. Kinetic analysis of human KAT II demonstrated its catalytic efficiency for individual amino-group donors and acceptors, providing information as to its preferred substrate affinity. Structural analysis of the human KAT II complex with alpha-oxoglutaric acid revealed a conformational change of an N-terminal fraction, residues 15-33, that is able to adapt to different substrate sizes, which provides a structural basis for its broad substrate specificity. << Less
Biosci. Rep. 28:205-215(2008) [PubMed] [EuropePMC]
This publication is cited by 26 other entries.
Comments
Mutli-step reaction: RHEA:69100 + RHEA:42452