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
2.6.1.21 D-amino-acid transaminaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.6.1.21 - D-amino-acid transaminase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A77T
site-directed mutagenesis, the mutation leads to defects in AA metabolism. The mutation A77T leads to a strong decrease in the production of D-Glu and D-Ala with 2-oxoglutarate or pyruvate as substrates, respectively. Instead, the enzymatic defect of AtDAT1(A77T) is quantitatively similar to that of AtDAT1(Ler)
A77T/T303S
naturally occuring mutation in Arabidopsis thaliana accession Ler, sequencing of the genomic locus and the cDNA of AtDAT1 from accession Ler reveals the two missense mutations leading to amino acid exchanges of the protein sequence (A77T and T303S), but solely the A77T amino acid exchange is responsible for the activity loss of AtDAT1(Ler)
T303S
site-directed mutagenesis, the mutant enzyme with the T303S amino acid exchange AtDAT1(T303S) shows an activity comparable to wild-type AtDAT1(Col-0)
A77T
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site-directed mutagenesis, the mutation leads to defects in AA metabolism. The mutation A77T leads to a strong decrease in the production of D-Glu and D-Ala with 2-oxoglutarate or pyruvate as substrates, respectively. Instead, the enzymatic defect of AtDAT1(A77T) is quantitatively similar to that of AtDAT1(Ler)
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A77T/T303S
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naturally occuring mutation in Arabidopsis thaliana accession Ler, sequencing of the genomic locus and the cDNA of AtDAT1 from accession Ler reveals the two missense mutations leading to amino acid exchanges of the protein sequence (A77T and T303S), but solely the A77T amino acid exchange is responsible for the activity loss of AtDAT1(Ler)
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T303S
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site-directed mutagenesis, the mutant enzyme with the T303S amino acid exchange AtDAT1(T303S) shows an activity comparable to wild-type AtDAT1(Col-0)
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H86F
site-directed mutagenesis, the mutant shows no activity with (R)-PEA and no wild-type DATA activity
L201A
P119G/R120G/P121G
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higher activity than wild-type with both pyruvate and 2-oxoglutarate as amino acceptors and a variety of D-amino acids except for D-alanine and D-aspartate, reduced thermostability
S180A
site-directed mutagenesis, the mutant shows no activity with (R)-PEA and no wild-type DATA activity
Y31F
site-directed mutagenesis, the mutant shows low activity with (R)-PEA and good wild-type DATA activity
Y31F/H86F
site-directed mutagenesis, variant M2 exhibited some (R)-PEA acceptance when PMP formation after incubating the purified variant with (R)-PEA is assayed, which indicates a completed first half-reaction. Lack of activity in the acetophenone assay and with wild-type substrate
Y31F/H86F/S180A/T242I
site-directed mutagenesis, variant M2-4 shows significant activity toward (R)-PEA, and retains no native DATA activity
Y31F/H86F/Y88F
site-directed mutagenesis, variant M2-3 shows significant activity toward (R)-PEA and retains 34% of the native DATA activity
Y31F/H86F/Y88F/H100L/S180A/T242I
site-directed mutagenesis, variant M2-6 shows almost complete depletion of the native DATA activity but high activity toward (R)-phenylethylamine ((R)-PEA) and has a specific activity of 326 milliunits/mg in the conversion of (R)-PEA and pyruvate to acetophenone and D-alanine
Y31F/H86F/Y88F/S180A/T242I
site-directed mutagenesis, variant M2-5 shows significant activity toward (R)-PEA and partially retains native DATA activity
Y88E
site-directed mutagenesis, the mutant shows no activity with (R)-PEA and no wild-type DATA activity
Y88F
site-directed mutagenesis, the mutant shows low activity with (R)-PEA and no wild-type DATA activity
H86F
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site-directed mutagenesis, the mutant shows no activity with (R)-PEA and no wild-type DATA activity
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S180A
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site-directed mutagenesis, the mutant shows no activity with (R)-PEA and no wild-type DATA activity
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Y88E
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site-directed mutagenesis, the mutant shows no activity with (R)-PEA and no wild-type DATA activity
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Y88F
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site-directed mutagenesis, the mutant shows low activity with (R)-PEA and no wild-type DATA activity
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additional information
additional information
the accession M7323S displays a strongly reduced AtDAT1 transcript level. When this accession is grown on D-Met supplemented medium, defects in amino acid metabolism are observed similar to those found in accession Ler and the dat1 mutant seedlings. This defect is not just due to the reduced transcription of AtDAT1 in M7323S. Sequencing of the genomic locus and the cDNA of AtDAT1 from M7323S reveals that this gene contains a T->A mutation at genomic position +1259. This leads 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)
additional information
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the accession M7323S displays a strongly reduced AtDAT1 transcript level. When this accession is grown on D-Met supplemented medium, defects in amino acid metabolism are observed similar to those found in accession Ler and the dat1 mutant seedlings. This defect is not just due to the reduced transcription of AtDAT1 in M7323S. Sequencing of the genomic locus and the cDNA of AtDAT1 from M7323S reveals that this gene contains a T->A mutation at genomic position +1259. This leads 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)
additional information
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the accession M7323S displays a strongly reduced AtDAT1 transcript level. When this accession is grown on D-Met supplemented medium, defects in amino acid metabolism are observed similar to those found in accession Ler and the dat1 mutant seedlings. This defect is not just due to the reduced transcription of AtDAT1 in M7323S. Sequencing of the genomic locus and the cDNA of AtDAT1 from M7323S reveals that this gene contains a T->A mutation at genomic position +1259. This leads 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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additional information
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replacement of the loop core P119-R120-P121 with glycine chains of different lengths: 1, 3, or 5 glycines, mutant forms are much more active than the wild type enzyme in the overall reactions with various amino acids and pyruvate
additional information
creation of an (R)-amine transaminase activity within an alpha-amino acid transaminase scaffold via one to six amino acid substitutions in the enzyme's active site. The final sextuple variant M2-6 shows almost complete depletion of the native DATA activity but high activity toward (R)-phenylethylamine ((R)-PEA) and has a specific activity of 326 milliunits/mg in the conversion of (R)-PEA and pyruvate to acetophenone and D-alanine. The crystal structure of the D-amino acid aminotransferase (DATA, UniProt ID P19938, EC 2.6.1.21) from Bacillus sp. strain YM-1 (PDB entry 3DAA) is used as a scaffold for the computational enzyme redesign. Molecular dynamics simulations and molecular mechanics Poisson-Boltzmann surface area (MM/PBSA) calculations
additional information
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creation of an (R)-amine transaminase activity within an alpha-amino acid transaminase scaffold via one to six amino acid substitutions in the enzyme's active site. The final sextuple variant M2-6 shows almost complete depletion of the native DATA activity but high activity toward (R)-phenylethylamine ((R)-PEA) and has a specific activity of 326 milliunits/mg in the conversion of (R)-PEA and pyruvate to acetophenone and D-alanine. The crystal structure of the D-amino acid aminotransferase (DATA, UniProt ID P19938, EC 2.6.1.21) from Bacillus sp. strain YM-1 (PDB entry 3DAA) is used as a scaffold for the computational enzyme redesign. Molecular dynamics simulations and molecular mechanics Poisson-Boltzmann surface area (MM/PBSA) calculations
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additional information
construction of a synthetic gene coding the transaminase Dret from Desulfohalobium retbaense. The following structures are chosen as the templates for constructing the Dret model: (a) (R)-TA from Nectria haematococca (PDB ID 4CMD) residues 7-44 for the modeling of the N-terminus of Dret (identity of 22%), (b) DAAT from Bacillus sp. YM-1 (bsDAAT, PDB ID 3DAA) residues 45-302 (identity of 26%), (c) BCAT from Geoglobus acetivorans (PDB ID 5E25) residues 302-314 (identity of 28%). The amino acid sequences required for modeling by homology are fitted. Comparing the structure of Dret with the structure of the canonical bsDAAT (PDB ID 3DAA) shows a series of differences in the structure of the active sites
additional information
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construction of a synthetic gene coding the transaminase Dret from Desulfohalobium retbaense. The following structures are chosen as the templates for constructing the Dret model: (a) (R)-TA from Nectria haematococca (PDB ID 4CMD) residues 7-44 for the modeling of the N-terminus of Dret (identity of 22%), (b) DAAT from Bacillus sp. YM-1 (bsDAAT, PDB ID 3DAA) residues 45-302 (identity of 26%), (c) BCAT from Geoglobus acetivorans (PDB ID 5E25) residues 302-314 (identity of 28%). The amino acid sequences required for modeling by homology are fitted. Comparing the structure of Dret with the structure of the canonical bsDAAT (PDB ID 3DAA) shows a series of differences in the structure of the active sites
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additional information
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construction of a synthetic gene coding the transaminase Dret from Desulfohalobium retbaense. The following structures are chosen as the templates for constructing the Dret model: (a) (R)-TA from Nectria haematococca (PDB ID 4CMD) residues 7-44 for the modeling of the N-terminus of Dret (identity of 22%), (b) DAAT from Bacillus sp. YM-1 (bsDAAT, PDB ID 3DAA) residues 45-302 (identity of 26%), (c) BCAT from Geoglobus acetivorans (PDB ID 5E25) residues 302-314 (identity of 28%). The amino acid sequences required for modeling by homology are fitted. Comparing the structure of Dret with the structure of the canonical bsDAAT (PDB ID 3DAA) shows a series of differences in the structure of the active sites
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additional information
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construction of a synthetic gene coding the transaminase Dret from Desulfohalobium retbaense. The following structures are chosen as the templates for constructing the Dret model: (a) (R)-TA from Nectria haematococca (PDB ID 4CMD) residues 7-44 for the modeling of the N-terminus of Dret (identity of 22%), (b) DAAT from Bacillus sp. YM-1 (bsDAAT, PDB ID 3DAA) residues 45-302 (identity of 26%), (c) BCAT from Geoglobus acetivorans (PDB ID 5E25) residues 302-314 (identity of 28%). The amino acid sequences required for modeling by homology are fitted. Comparing the structure of Dret with the structure of the canonical bsDAAT (PDB ID 3DAA) shows a series of differences in the structure of the active sites
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additional information
-
construction of a synthetic gene coding the transaminase Dret from Desulfohalobium retbaense. The following structures are chosen as the templates for constructing the Dret model: (a) (R)-TA from Nectria haematococca (PDB ID 4CMD) residues 7-44 for the modeling of the N-terminus of Dret (identity of 22%), (b) DAAT from Bacillus sp. YM-1 (bsDAAT, PDB ID 3DAA) residues 45-302 (identity of 26%), (c) BCAT from Geoglobus acetivorans (PDB ID 5E25) residues 302-314 (identity of 28%). The amino acid sequences required for modeling by homology are fitted. Comparing the structure of Dret with the structure of the canonical bsDAAT (PDB ID 3DAA) shows a series of differences in the structure of the active sites
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