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
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1.4.1.16
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glutamicum
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corynebacterium
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d-amino
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deamination
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thermophilum
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symbiobacterium
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l-lysine
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dihydrodipicolinate
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2-keto
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thermosphaericus
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ureibacillus
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isoxazoline
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homoserine
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sphaericus
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synthesis
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biotechnology
- 1.4.1.16
- glutamicum
- corynebacterium
-
d-amino
-
deamination
- thermophilum
- symbiobacterium
- l-lysine
- dihydrodipicolinate
-
2-keto
- thermosphaericus
-
ureibacillus
-
isoxazoline
- homoserine
- sphaericus
- synthesis
- biotechnology
Reaction
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
Advanced search results
Engineering
Engineering on EC 1.4.1.16 - diaminopimelate dehydrogenase
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Q154L/T173I/R199M/P248S/H249N/N276S
A69R
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
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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+
R71A
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
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
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the mutant shows reduced catalytic efficiency with meso-2,6-diaminoheptanedioate and NADP+ compared to the wild type enzyme
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R71A
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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
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Q154L/D158G/T173I/R199M/H249N
additional information
the mutant shows strongly reduced deamination activity with meso-2,6-diaminoheptanedioate and increased animation activity with pyruvate, phenylpyruvate, and 4-methyl-2-oxopentanoic acid compared to the wild type enzyme
Q154L/T173I/R199M/P248S/H249N/N276S
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the mutant shows strongly reduced deamination activity with meso-2,6-diaminoheptanedioate and increased animation activity with pyruvate, phenylpyruvate, and 4-methyl-2-oxopentanoic acid compared to the wild type enzyme
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mutation to the correspondung residue of Symbiobacteium thermophilum DAPDH. Mutation improves the catalytic efficiencies toward 2-keto acids and does not affect the catalytic efficiency toward meso-DAP
A69R
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mutation to the correspondung residue of Symbiobacteium thermophilum DAPDH. Mutation improves the catalytic efficiencies toward 2-keto acids and does not affect the catalytic efficiency toward meso-DAP
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site-directed saturation mutagenesis, the mutant shows 35.1fold increased activity with phenylpyruvate compared to the wild-type enzyme
H227V
mutant shows high activity toward phenylpyruvic acid and 2-oxo-4-phenylbutyric acid
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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
R71A
mutation destroys the cation-pi interaction between residues R71 and Y205
construction of a thermostable, NADP+-dependent D-amino acid dehydrogenase (DAADH) from the meso-diaminopimelate dehydrogenase of strain A1 by introducing five point mutations into amino acid residues located in the active site. In the presence of NADP+, the mutant enzyme catalyzes the oxidative deamination of several D-amino acids, including D-cyclohexylalanine, D-isoleucine, and D-2-aminooctanoate, but not of meso-diaminopimelate. The corresponding 2-oxo acids are aminated in the presence of NADPH and ammonia in the reverse reaction, mutant substrate specificity, overview. The mutant enzyme is also more thermostable than its parental meso-diaminopimelate dehydrogenase
Q154L/D158G/T173I/R199M/H249N
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construction of a thermostable, NADP+-dependent D-amino acid dehydrogenase (DAADH) from the meso-diaminopimelate dehydrogenase of strain A1 by introducing five point mutations into amino acid residues located in the active site. In the presence of NADP+, the mutant enzyme catalyzes the oxidative deamination of several D-amino acids, including D-cyclohexylalanine, D-isoleucine, and D-2-aminooctanoate, but not of meso-diaminopimelate. The corresponding 2-oxo acids are aminated in the presence of NADPH and ammonia in the reverse reaction, mutant substrate specificity, overview. The mutant enzyme is also more thermostable than its parental meso-diaminopimelate dehydrogenase
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systems-wide metabolic pathway engineering in Corynebacterium glutamicum for bio-based production of diaminopentane. Superior strains with desirable properties such as (i) the release from unwanted feedback regulation at the level of aspartokinase and pyruvate carboxylase by introducing the point mutations lysC311 and pycA458, (ii) an optimized supply of the key precursor oxaloacetate by amplifying the anaplerotic enzyme, pyruvate carboxylase, and deleting phosphoenolpyruvate carboxykinase which otherwise removes oxaloacetate, (iii) enhanced biosynthetic flux via combined amplification of aspartokinase, dihydrodipicolinate reductase, diaminopimelate dehydrogenase and diaminopimelate decarboxylase, and (iv) attenuated flux into the threonine pathway competing with production by the leaky mutation hom59 in the homoserine dehydrogenasegene
additional information
in order to enlarge the substrate binding pocket of the meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum to accommodate larger 2-keto acids, e.g. phenylalanine, four amino acid residues, Phe146, Thr171, Arg181, and His227, are targeted for site saturation mutagenesis
additional information
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in order to enlarge the substrate binding pocket of the meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum to accommodate larger 2-keto acids, e.g. phenylalanine, four amino acid residues, Phe146, Thr171, Arg181, and His227, are targeted for site saturation mutagenesis