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H121R
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isoform 2, 80% increase in ornithine dependent activity, 64% decrease in canaline-dependent activity
R54G
site-directed mutagenesis, inactive mutant, not exhibiting any PTC or OTC activity
Y230V/G231S/L232M/Y233G
engineering of the 230-loop of the enzyme, by replacing the sequence 230YGLY233 of the putrescine signature by its OTC counterpart VSMG, favors the use of ornithine and impairs that of putrescine
C273A
the mutant shows 2.8 and 3.2fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
D140N
the mutant shows 5.4 and 28fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
D231A
the mutant shows 450 and 580fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
E299D
the mutant shows 2.5 and 4.2fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
E299Q
the mutant shows 110 and 51fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
H272L
the mutant shows 310 and 120fold and decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
H272N
the mutant shows 4.2 and 3.4fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Q104L
the mutant shows 5.9 and 10fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Q106E
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mutant to study the carbamoyl phosphate cooperativity on the anabolic OTCase
R57A
the mutant shows 57 and 44fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
S61A
the mutant shows 6.1 and 1.8fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y160F
the mutant shows 6.7 and 8.2fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y160S
the mutant shows 1.5 and 14fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y229F
the mutant shows 3.5 and 2.7fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y229S
the mutant shows 1.7 and 1.4fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
K88Q
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less than 1% of wild-type activity
K88R
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mutant retains substantial enzymatic activity
R277W
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shows no substrate inhibition by ornithine, 70fold lower affinity for L-ornithine
E106A
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mutant arcB6240, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
E106G
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mutant arcB6254, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
E106A
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mutant arcB6240, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
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E106G
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mutant arcB6254, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
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A240D
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10fold increase of Km at 55°C
E277G
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14fold increase of Km at 55°C
Y227D
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slight increase of Km at 55°C
D182N
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greatly reduced affinity for L-ornithine, no interaction with arginase
E123A
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little change in activity, or in sensitivity to arginase
E123S
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little change in activity, or in sensitivity to arginase
E256A
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greatly reduced affinity for L-ornithine, impaired interaction with arginase
E256Q
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greatly reduced affinity for L-ornithine, impaired interaction with arginase
G181R
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no residual activity
K260A
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important in mediating sensitivity to L-ornithine and arginase
K260R
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important in mediating sensitivity to L-ornithine and arginase
K263R
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important in mediating sensitivity to L-ornithine and arginase
K265A
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important in mediating sensitivity to L-ornithine and arginase
K265R
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important in mediating sensitivity to L-ornithine and arginase
K268A
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important in mediating sensitivity to L-ornithine and arginase
K268R
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important in mediating sensitivity to L-ornithine and arginase
K289S
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greatly reduced affinity for L-ornithine, impaired interaction with arginase
L290Q
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reduced activity, little change in sensitivity to arginase
L290S
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reduced activity, little change in sensitivity to arginase
N184Q
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greatly reduced affinity for L-ornithine, impaired interaction with arginase
N185Q
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greatly reduced affinity for L-ornithine, impaired interaction with arginase
Q294P
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little change in activity, or in sensitivity to arginase
T68G
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greatly reduced activity, no change in sensitivity to arginase
L118M
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isoform 2, 515% increase in ornithine dependent activity, 54% decrease in canaline-dependent activity
L118M
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isoform 2, 617% increase in ornithine dependent activity, 55% decrease in canaline-dependent activity
E105G
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no cooperativity towards carbamoyl phosphate, follows Michaelis-Menten kinetics
E105G
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mutant blocked in the active R (relaxed) state
additional information
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construction of the putrescine-producing strain PUT1 by deletion of argF, the gene for ornithine transcarbamoylase, and argR, encoding the L-arginine repressor, combined with heterologous expression of the Escherichia coli gene for L-ornithine decarboxylase SpeC. The strain requires supplementation of L-arginine and shows growth-decoupled putrescine production. By fine-tuning argF expression through modifications of the promoter, the translational start codon and/or the ribosome binding site, high productivity and titer can be obtained, optimization of putrescine production by mutant strains, overview
additional information
confirmation of decreased stability of the trimer of the enzyme lacking the C-terminal helix by deleting this helix
additional information
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screening and analysis of naturally occuring mutations and polymorphisms in the OTC gene, defects in the OTC gene cause a block in ureagenesis resulting in hyperammonemia, which can lead to brain damage and death, phenotypes of mutated individuals, overview
additional information
computer model of molecular dynamic
additional information
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construction of a lmo0036 knockout mutant by homologous recombination using for in-frame deletion of the whole length of lmo0036
additional information
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construction of a lmo0036 knockout mutant by homologous recombination using for in-frame deletion of the whole length of lmo0036
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additional information
generation of in-frame deletion mutants of ArgK
additional information
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generation of in-frame deletion mutants of ArgK
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additional information
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null mutant of argK encoding phaseolotoxin resistant isozyme, enzyme expression is independent of temperature and regulated directly by a compound resembling the inorganic moiety of phaseolotoxin