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1.4.1.16: diaminopimelate dehydrogenase

This is an abbreviated version!
For detailed information about diaminopimelate dehydrogenase, go to the full flat file.

Word Map on EC 1.4.1.16

Reaction

meso-2,6-diaminoheptanedioate
+
H2O
+
NADP+
=
L-2-amino-6-oxoheptanedioate
+
NH3
+
NADPH
+
H+

Synonyms

BAB07799, BF3690, DAPDH, DDH, meso-2,6-diaminopimelate dehydrogenase, meso-alpha,epsilon-diaminopimelate dehydrogenase, meso-DAPDH, meso-diaminopimelate dehydrogenase, NADP+-dependent meso-diaminopimelate dehydrogenase, Sth1425, Theth_1310

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                1.4.1.16 diaminopimelate dehydrogenase

Engineering

Engineering on EC 1.4.1.16 - diaminopimelate dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q154L/T173I/R199M/P248S/H249N/N276S
F146W
site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates
F146W/M152Q
site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates
H227C
site-directed saturation mutagenesis, the mutant shows 15.1fold increased activity with phenylpyruvate compared to the wild-type enzyme
H227I
mutant accepts substrates D-2-phenylglycine and D-homophenylalanine
H227V
K159R
mutation decreases the kcat/KM value with meso-DAP, the catalytic efficiency toward pyruvic acid increases by 24%
M152A
the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and reduced activity towards pyruvate compared to the wild type enzyme
M152H
the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and no activity towards pyruvate compared to the wild type enzyme
M152K
the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and reduced activity towards pyruvate compared to the wild type enzyme
M152L
the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and pyruvate compared to the wild type enzyme
M152N
the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and reduced activity towards pyruvate compared to the wild type enzyme
M152Q
site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates
M152S
the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and reduced activity towards pyruvate compared to the wild type enzyme
P69G
mutation results in decrease of kcat/KM with meso-DAP and pyruvic acid
R181F
site-directed saturation mutagenesis, the mutant shows 6.4fold increased activity with phenylpyruvate compared to the wild-type enzyme
R181F/H227V
site-directed saturation mutagenesis, the mutant shows 19.3fold increased activity with phenylpyruvate compared to the wild-type enzyme
R35S
-
the mutant shows reduced catalytic efficiency with meso-2,6-diaminoheptanedioate and NADP+ compared to the wild type enzyme
R35S/R36V
the mutations significantly lower the specific activity toward NADP+ compared to the wild type enzyme. The mutant enzyme favors NAD+ over NADP+
R71E
for reductive amination, the mutant shows a 1.5fold increase in Km and 0.24fold decrease in kcat. For oxidative deamination, a 50% decrease in the kcat/Km value is observed
R71I
R71I shows 0.37fold decrease in kcat/Km value for pyruvic acid
R71K
the kcat/Km values toward pyruvic acid and meso-DAP increase by 1.4fold and 1.8fold, respectively
R71Q
the kcat/Km values toward pyruvic acid and meso-DAP both decrease by 30%
R71S
for pyruvic acid, R71S shows few changes in kcat/Km values
S90T
mutation results in decrease of kcat/KM with meso-DAP and pyruvic acid
T171H
mutant accepts substrates D-2-phenylglycine and D-homophenylalanine
T171P
site-directed saturation mutagenesis, the mutant shows 2.2fold increased activity with phenylpyruvate compared to the wild-type enzyme
T171S
site-directed saturation mutagenesis, the mutant shows 2.8fold increased activity with phenylpyruvate compared to the wild-type enzyme
T171S/H227V
site-directed saturation mutagenesis, the mutant shows 10.6fold increased activity with phenylpyruvate compared to the wild-type enzyme
T171S/R181F
site-directed saturation mutagenesis, the mutant shows 4.0fold increased activity with phenylpyruvate compared to the wild-type enzyme
T171S/R181F/H227V
site-directed saturation mutagenesis, the mutant shows 14.6fold increased activity with phenylpyruvate compared to the wild-type enzyme
T70S
catalytic ability of T70S does not change much
V14L
mutation results in decrease of kcat/KM with meso-DAP and pyruvic acid
V156D
mutation results in decrease of kcat/KM with meso-DAP and pyruvic acid, almost complete loss of catalytic ability
V68M
mutation decreases the kcat/KM value with meso-DAP, the catalytic efficiency toward pyruvic acid does not change
W121L
mutant accepts substrates D-2-phenylglycine and D-homophenylalanine
W121L/H227I
mutant sow improved enzyme activities towards various 2-oxoacids including sterically bulky substrates. The substrate binding cavity of the mutant enzyme is reshaped to accommodate these bulky substrates, thus leading to higher enzyme activity
R35S
-
the mutant shows reduced catalytic efficiency with meso-2,6-diaminoheptanedioate and NADP+ compared to the wild type enzyme
-
R71A
-
the mutant shows about wild type catalytic efficiency with meso-2,6-diaminoheptanedioate and increased catalytic efficiency with NADP+ compared to the wild type enzyme
-
Q154L/D158G/T173I/R199M/H249N
additional information