Reaction participants Show >> << Hide
- 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 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-tyrosine Identifier CHEBI:58315 Charge 0 Formula C9H11NO3 InChIKeyhelp_outline OUYCCCASQSFEME-QMMMGPOBSA-N SMILEShelp_outline [NH3+][C@@H](Cc1ccc(O)cc1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 53 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-(4-hydroxyphenyl)pyruvate Identifier CHEBI:36242 (Beilstein: 3950858) help_outline Charge -1 Formula C9H7O4 InChIKeyhelp_outline KKADPXVIOXHVKN-UHFFFAOYSA-M SMILEShelp_outline Oc1ccc(CC(=O)C([O-])=O)cc1 2D coordinates Mol file for the small molecule Search links Involved in 20 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 122 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:47084 | RHEA:47085 | RHEA:47086 | RHEA:47087 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae.
Heilbronn J., Wilson J., Berger B.J.
An aminotransferase which catalyzes the final step in methionine recycling from methylthioadenosine, the conversion of alpha-ketomethiobutyrate to methionine, has been purified from Klebsiella pneumoniae and characterized. The enzyme was found to be a homodimer of 45-kDa subunits, and it catalyzed ... >> More
An aminotransferase which catalyzes the final step in methionine recycling from methylthioadenosine, the conversion of alpha-ketomethiobutyrate to methionine, has been purified from Klebsiella pneumoniae and characterized. The enzyme was found to be a homodimer of 45-kDa subunits, and it catalyzed methionine formation primarily using aromatic amino acids and glutamate as the amino donors. Histidine, leucine, asparagine, and arginine were also functional amino donors but to a lesser extent. The N-terminal amino acid sequence of the enzyme was determined and found to be almost identical to the N-terminal sequence of both the Escherichia coli and Salmonella typhimurium tyrosine aminotransferases (tyrB gene products). The structural gene for the tyrosine aminotransferase was cloned from K. pneumoniae and expressed in E. coli. The deduced amino acid sequence displayed 83, 80, 38, and 34% identity to the tyrosine aminotransferases from E. coli, S. typhimurium, Paracoccus denitrificans, and Rhizobium meliloti, respectively, but it showed less than 13% identity to any characterized eukaryotic tyrosine aminotransferase. Structural motifs around key invariant residues placed the K. pneumoniae enzyme within the Ia subfamily of aminotransferases. Kinetic analysis of the aminotransferase showed that reactions of an aromatic amino acid with alpha-ketomethiobutyrate and of glutamate with alpha-ketomethiobutyrate proceed as favorably as the well-known reactions of tyrosine with alpha-ketoglutarate and tyrosine with oxaloacetate normally associated with tyrosine aminotransferases. The aminotransferase was inhibited by the aminooxy compounds canaline and carboxymethoxylamine but not by substrate analogues, such as nitrotyrosine or nitrophenylalanine. << Less
J. Bacteriol. 181:1739-1747(1999) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.