EC Number   |
General Information |
Reference |
|---|
    2.6.1.21 | evolution |
diversity of D-amino acid utilizing bacteria from Kongsfjorden, Arctic, and the metabolic pathways for seven D-amino acids, analysis of key genes predicted to be involved in D-amino acid catabolism in the bacterial strains, detailed overview |
-, 759235 |
| 2.6.1.21 | evolution |
transaminases with the fold type IV of the PLP binding domain vary in substrate specificity and include enzymes specific to both D- and L-amino acids. D-amino acid transaminases (DAATs), branched-chain L-amino acid transaminases (BCATs), and (R)-primary amine specific transaminases ((R)-TA) are distinguished among the enzymes with the fold type IV |
-, 759812 |
| 2.6.1.21 | malfunction |
the Arabidopsis accession Landsberg erecta (Ler, A77T/T303S) is defective in metabolizing D-amino acids. Atdat1 loss-of-function mutants and Arabidopsis accessions with defective AtDAT1 alleles are unable to produce the metabolites of D-Met, D-Ala, D-Glu, and L-Met. Germination of seedlings in light and dark leads to enhanced growth inhibition of atdat1 mutants on D-Met. Ethylene measurements reveal an increased D-AA stimulated ethylene production in these mutants. D-Met is preferentially malonylated instead of the ethylene precursor 1-aminocyclopropane-1-carboxylic acid (ACC). This decrease of ACC degradation should then lead to the increase of ethylene production. A reciprocal relation of malonylated methionine and ACC upon D-Met application and significantly more malonyl-methionine is observed in atdat1 mutants. Unexpectedly, the malonyl-ACC levels do not differ between mutants and wild-type. The accession M7323S displays a strongly reduced AtDAT1 transcript level due to a nonsense mutation at the third position of a cysteine codon (TGT) to a stop codon (TGA) at position 248 of the AA sequence (C248STOP) |
-, 759259 |
| 2.6.1.21 | metabolism |
AtDAT1 is the central enzyme of plant D-amino acid (D-AA) metabolism |
-, 759259 |
| 2.6.1.21 | metabolism |
the enzyme is involved int he D-Ala and D-Asp metabolism in strain SM1922 of the arctic ocean bacterium. Pathways for D-Leu, D-Met, D-Phe, D-Thr, D-Tyr, D-Ser, and D-Asp metabolism in the isolated marine bacteria, overview |
-, 759235 |
| 2.6.1.21 | more |
molecular mechanism of stereospecificity toward D-leucine of the transaminase from Desulfohalobium retbaense, molecular dynamic simulations, overview. HOmology modeling using the structure of the canonical bsDAAT (PDB ID 3DAA) revealing a series of differences in the structure of the active sites |
-, 759812 |
| 2.6.1.21 | physiological function |
AtDAT1 is a key enzyme of D-amino acid stimulated ethylene production in Arabidopsis thaliana |
-, 759259 |
