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2.6.1.76: diaminobutyrate-2-oxoglutarate transaminase

This is an abbreviated version!
For detailed information about diaminobutyrate-2-oxoglutarate transaminase, go to the full flat file.

Word Map on EC 2.6.1.76

Reaction

L-2,4-diaminobutanoate
+
2-oxoglutarate
=
L-aspartate 4-semialdehyde
 +
L-glutamate

Synonyms

(Pl)EctB, 2,4-diaminobutyrate 4-aminotransferase, 2,4-diaminobutyrate aminotransferase, DABA aminotransferase, DABA AT, DABA-AT, DABA:2-KG 4 aminotransferase, Diaminobutyrate transaminase, EctB, L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase, L-diaminobutyric acid transaminase, More

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.76 diaminobutyrate-2-oxoglutarate transaminase

Engineering

Engineering on EC 2.6.1.76 - diaminobutyrate-2-oxoglutarate transaminase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D180V
about 2fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
D180V/E36V
double mutant displays less activity than mutant D180V
D180V/F320Y/Q325R
about 2.1-3.3fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
E36V
about 1.5fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
D180V
-
about 2fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
-
D180V/E36V
-
double mutant displays less activity than mutant D180V
-
D180V/F320Y/Q325R
-
about 2.1-3.3fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
-
E36V
-
about 1.5fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
-
K274A
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive
K274H
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive. This amino acid substitution does not affect the quaternary assembly of the mutant protein
K274R
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive
K274A
-
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive
-
K274H
-
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive. This amino acid substitution does not affect the quaternary assembly of the mutant protein
-
K274R
-
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive
-