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E211S
crystallization data, decrease in kcat, decrease in Km-value for 2-oxoglutarate
E211S/I50G
drastic decrease in kcat-value
E211S/I50G/C77K
10fold increase in decarboxylation activity
E211S/I50G/C77R
drastic decrease in kcat-value
E211S/I50H/V80D
10fold increase in decarboxylation activity, change of reaction specificity to that of a decarboxylase
E211S/I50H/V80T
decrease in kcat, decrease in Km-value for 2-oxoglutarate
E211S/I50N/V80D
drastic decrease in kcat-value
E211S/I50N/V80T
drastic decrease in kcat-value
E211S/I50Q/G295Y/V241A
drastic decrease in kcat-value
I50Q
crystallization data, decrease in kcat, increase in Km-values
I50Q/G295Y
decrease in kcat, decrease in Km-value for 2-oxoglutarate
V241A
crystallization data, decrease in kcat, decrease in Km-value for 2-oxoglutarate
C321M
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no enzymic activity, behaves as monomer even in absence of 2-mercaptoethanol
C321S
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no enzymic activity, behaves as monomer even in absence of 2-mercaptoethanol
K357A
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no enzymic activity, even not by addition of exogenous pyridoxal 5-phosphate
K357B
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no enzymic activity, even not by addition of exogenous pyridoxal 5-phosphate
K357N
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no enzymic activity, even not by addition of exogenous pyridoxal 5-phosphate
K357Q
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no enzymic activity, even not by addition of exogenous pyridoxal 5-phosphate
L211F
homozygous missense mutation idientified in in a family with encephalomyopathic mitochondrial DNA depletion syndrome
K274A
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
K274H
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is 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 is catalytically inactive
K274A
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site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
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K274R
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site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
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K330R
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no catalytic activity, no pyridoxal 5'-phosphate covalently linked to protein
synthesis
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simultaneous expression of gamma-aminobutyric acid aminotransferase gabT and succinic semialdehyde dehydrogenase gabD genes in Escherichia coli. The mixture of both enzymes, called GABase, is the key enzyme for the enzymatic analysis of GABA
synthesis
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simultaneous expression of gamma-aminobutyric acid aminotransferase gabT and succinic semialdehyde dehydrogenase gabD genes in Escherichia coli. The mixture of both enzymes, called GABase, is the key enzyme for the enzymatic analysis of GABA
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additional information
Agrobacterium tumefaciens is used to mediate inter-kingdom DNA transfer in plant genetic engineering. Gamma-aminobutyric acid (GABA) is a negative factor in the Agrobacterium-plant interaction, because it inhibits the DNA transfer. Generation of an Agrobacterium tumefaciens strain expressing the Escherichia coli gene gabT, which introduces GABA transaminase activity and the ability to degrade GABA, is achieved to circumvent the inhibitory effect of GABA. GabT activity enhances the T-DNA transfer ability of Agrobacterium tumefaciens
additional information
Agrobacterium tumefaciens is used to mediate inter-kingdom DNA transfer in plant genetic engineering. Gamma-aminobutyric acid (GABA) is a negative factor in the Agrobacterium-plant interaction, because it inhibits the DNA transfer. Generation of an Agrobacterium tumefaciens strain expressing the Escherichia coli gene gabT, which introduces GABA transaminase activity and the ability to degrade GABA, is achieved to circumvent the inhibitory effect of GABA. GabT activity enhances the T-DNA transfer ability of Agrobacterium tumefaciens
additional information
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Agrobacterium tumefaciens is used to mediate inter-kingdom DNA transfer in plant genetic engineering. Gamma-aminobutyric acid (GABA) is a negative factor in the Agrobacterium-plant interaction, because it inhibits the DNA transfer. Generation of an Agrobacterium tumefaciens strain expressing the Escherichia coli gene gabT, which introduces GABA transaminase activity and the ability to degrade GABA, is achieved to circumvent the inhibitory effect of GABA. GabT activity enhances the T-DNA transfer ability of Agrobacterium tumefaciens
additional information
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Agrobacterium tumefaciens is used to mediate inter-kingdom DNA transfer in plant genetic engineering. Gamma-aminobutyric acid (GABA) is a negative factor in the Agrobacterium-plant interaction, because it inhibits the DNA transfer. Generation of an Agrobacterium tumefaciens strain expressing the Escherichia coli gene gabT, which introduces GABA transaminase activity and the ability to degrade GABA, is achieved to circumvent the inhibitory effect of GABA. GabT activity enhances the T-DNA transfer ability of Agrobacterium tumefaciens
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additional information
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Agrobacterium tumefaciens is used to mediate inter-kingdom DNA transfer in plant genetic engineering. Gamma-aminobutyric acid (GABA) is a negative factor in the Agrobacterium-plant interaction, because it inhibits the DNA transfer. Generation of an Agrobacterium tumefaciens strain expressing the Escherichia coli gene gabT, which introduces GABA transaminase activity and the ability to degrade GABA, is achieved to circumvent the inhibitory effect of GABA. GabT activity enhances the T-DNA transfer ability of Agrobacterium tumefaciens
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additional information
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mutants of GABA transaminase suppress the severe phenotype of succinic semialdehyde dehydrogenase mutants in Arabidopsis
additional information
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the GABA transaminase loss-of-function mutant pop2-1 is oversensitive to ionic stress but not to osmotic stress
additional information
construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
additional information
construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
additional information
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
additional information
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
additional information
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. Method optimization and evaluation. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation on of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain KCTC H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview
additional information
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construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
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additional information
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construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
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additional information
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construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
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construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
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construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
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construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
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construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
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construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
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C-terminal mutant lacking 5 amino acids, no interference with kinetical parameters or functional properties but change in stability of dimeric structure at acidic pH