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C141S
reductive amination activity of C141S alone is insensitive to treatment with 2-hydroxyethyl disulfide
C415S
mutant loses its reductive amination activity in a manner very similar to the native enzyme
K116A
almost complete loss of activity
K128A
almost complete loss of activity
K136A
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH, fourfold increase in the Km value for NADH with a concomitant 1.6fold increase in the kcat value
K92A
almost complete loss of activity
N347A
almost complete loss of activity
R208A
almost complete loss of activity
R290A
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
S265A
residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
S379A
almost complete loss of activity
K116A
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almost complete loss of activity
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K128A
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almost complete loss of activity
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K92A
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almost complete loss of activity
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R208A
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almost complete loss of activity
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S379A
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almost complete loss of activity
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K136A
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residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH, fourfold increase in the Km value for NADH with a concomitant 1.6fold increase in the kcat value
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R290A
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residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
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S265A
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residue is directly involved in binding the 2'-phosphate group of NADP+, increase in Km value for NADPH
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C321A
site-directed mutagenesis, the mutant shows reduced NADP-related GDH activity, the mutation causes a greater than a 2fold drop in Vmax and more than a 2fold increase in Km for NADP+
K286Q
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q/S264L
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q/S264L/S240A
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
K341L
site-directed mutagenesis, the mutant shows reduced NADP-related GDH activity compared to wild-type
K92C
altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 5.5fold increase in speific activity with homoserine
K92M
altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 2.8fold increase in speific activity with homoserine
K92V
altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 7.2fold increase in speific activity with homoserine
P320A
site-directed mutagenesis, the mutant shows reduced NADP-related GDH activity, the mutation causes a greater than a 2fold drop in Vmax and more than a 2fold increase in Km for NADP+. The mutant is not inhibited by propylselen
R289Q
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
R292Q
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
K110L
a naturally occurring mutation responsible for the inactivation of the catalytic site of Gdh1
K419A
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site-directed mutagenesis of GDH1
K420A
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site-directed mutagenesis of GDH1
K423A
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site-directed mutagenesis of GDH1
K426A
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site-directed mutagenesis of GDH1
K110L
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a naturally occurring mutation responsible for the inactivation of the catalytic site of Gdh1
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K419A
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site-directed mutagenesis of GDH1
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K420A
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site-directed mutagenesis of GDH1
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K423A
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site-directed mutagenesis of GDH1
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K426A
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site-directed mutagenesis of GDH1
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E158Q
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3.3% as active as wild-type
T138E
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1.6% as active as wild-type
D167T
the mutant enzyme is slightly more thermostable than the wild-type enzyme
T138E
the mutant enzyme is much less thermostable than the wild-type enzyme
D167T
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the mutant enzyme is slightly more thermostable than the wild-type enzyme
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T138E
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the mutant enzyme is much less thermostable than the wild-type enzyme
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N117R
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80% activity of wild-type at optimum temperature for catalysis
R190A/E231A/K193A
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mutation has no effect on the overall conformation of the protein
S128R
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same activity as wild-type at optimum temperature for catalysis
S128R/T158E
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120% activity of wild-type at optimum temperature for catalysis
S128R/T158E/N117R
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same activity as wild-type at optimum temperature for catalysis
S128R/T158E/N117R/S160E
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same activity as wild-type at optimum temperature for catalysis
S128R/T158E/S160E
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same activity as wild-type at optimum temperature for catalysis
T158E
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60% activity of wild-type at optimum temperature for catalysis
additional information
generation of a BpNADPGDH II deletion mutant of Benjaminiella poitrasii (DELTAnadpgdh II::HygR) via Agrobacterium-mediated transformation of the BpNADPGDH II disruption cassette
additional information
generation of a BpNADPGDH II deletion mutant of Benjaminiella poitrasii (DELTAnadpgdh II::HygR) via Agrobacterium-mediated transformation of the BpNADPGDH II disruption cassette
additional information
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generation of a BpNADPGDH II deletion mutant of Benjaminiella poitrasii (DELTAnadpgdh II::HygR) via Agrobacterium-mediated transformation of the BpNADPGDH II disruption cassette
additional information
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an active chimera (CEC) consisting of the substrate-binding domain (domain I) of CsGDH and the coenzyme-binding domain (domain II) of Escherichia coli GDH is generated. Kinetic constants of chimeric protein: Km values for substrates L-glutamate, 2-oxoglutarate, NH4Cl highly increased compared to wild-type, Vmax values also highly increased compared to wild-type. The CEC chimera, like Escherichia coli GDH, has a marked preference for NADP(H) as coenzyme. selectivity for the phosphorylated coenzyme does indeed reside solely in domain II. Positive cooperativity toward L-glutamate, characteristic of wild-type CsGDH, retains with domain I. Although glutamate cooperativity occurs only at higher pH values in the wild-tpye CsGDH, the chimeric protein shows it over the full pH range explored. The chimera is capable of catalyzing severalfold higher reaction rates (Vmax) in both directions than either of the parent enzymes from which it is constructed
additional information
chimeric protein consisting of domain I from NAD+-dependent GDH of Clostridium symbiosum, residues 1-200, domain II from NADP+-dependent GDH of Escherichia coli, residues 201-404 and the C-terminal helix again from Clostridium symbiosum, residues 405-448 which re-enters domain I. Domain II maintains its structural and functional integrity independent of the hinge and domain I. The enzyme is fully functional and retains the preference for NADP+ cofactor from the parent E. coli domain II
additional information
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gdh mutant TIL487, loss of ability to degrade amino acids
additional information
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gdh mutant TIL487, loss of ability to degrade amino acids
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additional information
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disruption of the NADPH-dependent glutamate dehydrogenase gene leads to decreased beta-lactam production
additional information
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disruption of the NADPH-dependent glutamate dehydrogenase gene leads to decreased beta-lactam production
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additional information
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deletion mutant lacking the first 19 amino acid residues, shows unchanged activity and forms hexamers, thus the unique extension does not appear to be essential for catalysis and subunit assembly, and presumably fulfils some other yet unknown function
additional information
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construction of enzyme deletion mutants DELTAgdh1 and DELTAgdh3, the mutants show less than 20% of wild-type activity, genotypes and phenotypes, overview
additional information
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promoter swapping and site-directed mutagenesis of GDH1 and GDH3, construction of gene disruption null mutants of both genes, phenotypes and mutant activities, overview
additional information
mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3
additional information
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mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3
additional information
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mutational analysis shows that the N-terminal proximal region of Gdh1 is essential for glucose starvation-induced aggregation. The substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increases the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary-phase cells and the stationary phase-specific stress-sensitive phenotype of the mutants lacking Gdh3
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additional information
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promoter swapping and site-directed mutagenesis of GDH1 and GDH3, construction of gene disruption null mutants of both genes, phenotypes and mutant activities, overview
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additional information
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overexpression of an NADP(H)-dependent glutamate dehydrogenase gene, TrGDH, from Trichurus sp. improves nitrogen assimilation, growth status, and grain weight per plant in rice, phenotype, overview. Compared with the rice GDH (OsGDH4), TrGDH exhibits higher affinity for NH4+
additional information
YALI0F17820g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overvexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
additional information
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YALI0F17820g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overvexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
additional information
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YALI0F17820g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overvexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
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additional information
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YALI0F17820g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overvexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities
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