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A163S
site-directed mutagenesis, the mutant shows almost unaltered cofactor specificity compared to the wild-type enzyme
H171
site-directed mutagenesis, the mutant shows almost unaltered cofactor specificity compared to the wild-type enzyme
L351V
site-directed mutagenesis, the mutant shows unaltered cofactor specificity compared to the wild-type enzyme
Q350N
site-directed mutagenesis, the mutant shows 44fold increased activity with NAD+ compared to the wild-type enzyme and can also also utilize NADH efficiently. Unlike the wild-type enzyme, mutants Q350N and Q350N/H171A are able to synthesize L-homoserine from aspartate efficiently with NADH as a cofactor
Q350N/H171A Q350N
site-directed mutagenesis, the mutant shows 66fold increased activity with NAD+ compared to the wild-type enzyme and can also utilize NADH efficiently. Unlike the wild-type enzyme, mutants Q350N and Q350N/H171A are able to synthesize L-homoserine from aspartate efficiently with NADH as a cofactor
S138Q
site-directed mutagenesis, the mutant shows unaltered cofactor specificity compared to the wild-type enzyme
R267L
the mutant shows 9.5% activity compared to the wild type enzyme
C136S
site-directed mutagenesis, active site mutant is nearly inactive due to decrease in nuleophilicity, and also by a change in the orientation of the histidine imidazole ring
C136S
the mutation virtually eliminates catalysis
E243D
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site-directed mutagenesis, unaltered Km for the substrates but 8fold increased Km for cofactor NADP+, active site structural alterations
E243D
the mutant shows 1.2% activity compared to the wild type enzyme
H277N
site-directed mutagenesis, active site mutant shows 100fold decreased catalytic efficiency compared to the wild-type enzyme, shift in the position of the bound reaction intermediate
H277N
the mutant shows 1% activity compared to the wild type enzyme
K246R
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site-directed mutagenesis, mutation of a putative phosphate binding residue, unaltered substrate Km, active site structural alterations
K246R
the mutant shows 3.3% activity compared to the wild type enzyme
R103K
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site-directed mutagenesis, adversely affected interaction between enzyme and phosphate, active site structural alterations
R103K
the mutant shows 0.4% activity compared to the wild type enzyme
R103L
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site-directed mutagenesis, altered interaction between enzyme and phosphate, active site structural alterations
R103L
the mutant shows 0.07% activity compared to the wild type enzyme
R270K
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site-directed mutagenesis, active site mutant, unaltered substrate Km, active site structural alterations
R270K
the mutant shows 0.1% activity compared to the wild type enzyme
additional information
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construction of an gene asadh promoter-replacement mutant Mycobacterium tuberculosis strain, designated MTB::asadh, in which the asadh gene expression is regulated by pristinamycin. Bacterial growth is survival of MTB::asadh in host cells is completely inhibited in the absence of the inducer pristinamycin. The growth of the mutant is rigorously dependent on the presence of the inducer in the medium. The starved mutant exhibits a marked reduction (approximately 80%) in the cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview. With the addition of pristinamycin, the cell wall contents and morphology are recovered in a similar manner to those of the wild-type strain. The starved mutant also exhibits almost no pathogenicity in an in vitro model of infection using mouse macrophage J774A.1 cells. The mutant shows a concentration-dependent recovery of pathogenicity with the addition of the inducer
additional information
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construction of an gene asadh promoter-replacement mutant Mycobacterium tuberculosis strain, designated MTB::asadh, in which the asadh gene expression is regulated by pristinamycin. Bacterial growth is survival of MTB::asadh in host cells is completely inhibited in the absence of the inducer pristinamycin. The growth of the mutant is rigorously dependent on the presence of the inducer in the medium. The starved mutant exhibits a marked reduction (approximately 80%) in the cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview. With the addition of pristinamycin, the cell wall contents and morphology are recovered in a similar manner to those of the wild-type strain. The starved mutant also exhibits almost no pathogenicity in an in vitro model of infection using mouse macrophage J774A.1 cells. The mutant shows a concentration-dependent recovery of pathogenicity with the addition of the inducer
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additional information
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construction of and screening of a library of 2914 transposon-insertional mutants in the Staphylococcus aureus MW2 strain, identification of aspartate semialdehyde dehydrogenase (asd)-inactivated mutant, and inactivated mutants of lysA and thrC defective in lysine and threonine bioynthesis. Identification of Tn551 insertion sites, the Tn551 insertion sites of M3-91 and M17-9 are 276 bp and 347 bp from the initiation of the asd gene, respectively
additional information
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construction of and screening of a library of 2914 transposon-insertional mutants in the Staphylococcus aureus MW2 strain, identification of aspartate semialdehyde dehydrogenase (asd)-inactivated mutant, and inactivated mutants of lysA and thrC defective in lysine and threonine bioynthesis. Identification of Tn551 insertion sites, the Tn551 insertion sites of M3-91 and M17-9 are 276 bp and 347 bp from the initiation of the asd gene, respectively
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