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2.6.1.88 |
Description |
L-methionine transaminase |
Alternative names |
methionine-oxo-acid transaminase;
L-methionine:2-oxo-acid aminotransferase;
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Catalyzed reaction |
L-methionine + a 2-oxo carboxylate = 2-oxo-4-methylthiobutanoate + an L-amino acid |
Cofactor |
Pyridoxal-phosphate. |
Comments |
The enzyme is most active with L-methionine. It participates in the L-methionine salvage pathway from S-methyl-5'-thioadenosine, a by-product of polyamine biosynthesis. The enzyme from the bacterium Klebsiella pneumoniae can use several different amino acids as amino donor, with aromatic amino acids being the most effective [1]. The enzyme from the plant Arabidopsis thaliana is also a part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates [3]. |
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Family a includes only plant enzymes, beloging to the fold type IV group; they apparently represent specialized forms of branched-chain amino acid transaminases.
Family b includes enzymes that belong to the fold type I group and are from bacteria. |
PDB |
1u08; |
Organisms |
-Eubacteria -Plants |
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Family |
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Links |
Enzyme (activities) 2.6.1.88
BRENDA (activities) 2.6.1.88
KEGG (pathways) 2.6.1.88
PLPMDB (PLP mutants) 2.6.1.88
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References |
Schuster, J., Knill, T., Reichelt, M., Gershenzon, J. and Binder, S. (2006) Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis. Plant Cell 18 18 2664-79. Dolzan, M., Johansson, K., Roig-Zamboni, V., Campanacci, V., Tegoni, M., Schneider, G. and Cambillau, C. (2004) Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function. 571 141-6. Articles on 2.6.1.88 |
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last changed |
2017/07/11 17:29 |
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