2.6.1.21: D-amino-acid transaminase
This is an abbreviated version!
For detailed information about D-amino-acid transaminase, go to the full flat file.
Word Map on EC 2.6.1.21
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2.6.1.21
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pyridoxal
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racemase
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transamination
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d-glutamate
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pyridoxamine
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sphaericus
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quinonoid
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aldimine
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4-amino-4-deoxychorismate
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yoshimura
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ketimine
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pyridoxal-5'-phosphate-dependent
- 2.6.1.21
- pyridoxal
- racemase
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transamination
- d-glutamate
- pyridoxamine
- sphaericus
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quinonoid
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aldimine
- 4-amino-4-deoxychorismate
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yoshimura
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ketimine
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pyridoxal-5'-phosphate-dependent
Reaction
Synonyms
aminotransferase, D-alanine, AspFum, AspOry, AspTer, AtDAT1, D-AA transaminase, D-AAT, D-alanine aminotransferase, D-alanine transaminase, D-alanine:2-oxoglutarate aminotransferase, D-amino acid aminotransferase, D-amino acid transaminase, D-aspartate transaminase, D-aspartic aminotransferase, DAA aminotransferase, DAA transaminase, DAAT, DAT, DatA, Dret, Dret_1107, EC 2.6.1.10, FQP89_01185, GibZea, MSMEG_5795, MycVan, NeoFis, PenChr, TRA-01185
ECTree
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General Information
General Information on EC 2.6.1.21 - D-amino-acid transaminase
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evolution
malfunction
metabolism
physiological function
additional information
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
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
evolution
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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
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evolution
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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
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evolution
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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
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evolution
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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
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evolution
Halomonas titanicae SM1922
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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
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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)
malfunction
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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)
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AtDAT1 is the central enzyme of plant D-amino acid (D-AA) metabolism
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
metabolism
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AtDAT1 is the central enzyme of plant D-amino acid (D-AA) metabolism
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metabolism
Halomonas titanicae SM1922
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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
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AtDAT1 is a key enzyme of D-amino acid stimulated ethylene production in Arabidopsis thaliana
physiological function
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AtDAT1 is a key enzyme of D-amino acid stimulated ethylene production in Arabidopsis thaliana
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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
additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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