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D230N
the variant has somewhat greater processivity than the wild-type enzyme
E173K
the variant has somewhat greater processivity than the wild-type enzyme
E245K
mutation leads to very high polyP accumulation in vivo but is not different from the wild type in either activity or chain length of polyP produced in vitro
F488A
-
complete loss of all 4 polyphosphate kinase activities
P507A
-
complete loss of all 4 polyphosphate kinase activities
Q674A
-
complete loss of all 4 polyphosphate kinase activities
R375A
-
complete loss of all 4 polyphosphate kinase activities
R564A
-
complete loss of all 4 polyphosphate kinase activities
R621A
-
complete loss of all 4 polyphosphate kinase activities
S380A
-
complete loss of all 4 polyphosphate kinase activities
Y468A
-
120-140% of wild-type polyphosphate, GTP, and guanosine 5'-tetraphosphate synthesis activity, 20-50% of wild-type ATP synthesis activity
D230N
-
the variant has somewhat greater processivity than the wild-type enzyme
-
E173K
-
the variant has somewhat greater processivity than the wild-type enzyme
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E245K
-
mutation leads to very high polyP accumulation in vivo but is not different from the wild type in either activity or chain length of polyP produced in vitro
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D62A
-
about 1000fold decrease in activity
-
E126G
about 18% of wild-type activity with substrate AMP, about 40% of wild-type activity with ADP
E126N
about 5% of wild-type activity with substrate AMP, bout 15% of wild-type activity with ADP
E126G
-
about 18% of wild-type activity with substrate AMP, about 40% of wild-type activity with ADP
-
E126N
-
about 5% of wild-type activity with substrate AMP, bout 15% of wild-type activity with ADP
-
N121D
-
7fold decrease in activity with AMP, 25fold decrease in activity with ADP
-
A615S
-
the mutant exhibits about wild type activity for ATP synthesis and polyphosphate synthesis
E681A
-
the mutant exhibits less than 5% activity for ATP synthesis and less than 30% activity for polyphosphate synthesis compared o the wild type enzyme
F125A
the proteins has significantly reduced activity as compared to wild type protein
F67A
-
84% activity compared to the wild type enzyme
G69R
-
67.1% activity compared to the wild type enzyme
G72A
the activity of MBP-G72APPK-2 and wild type proteins are similar
G74R
-
7.6% activity compared to the wild type enzyme, the mutant enzyme cannot interact with nucleoside diphosphate kinase
H115A
-
49% activity compared to the wild type enzyme
H115A/H247A
-
6% activity compared to the wild type enzyme
H150A
-
the mutation causes PPK1 protein deficient but not defective in autophosphorylation and severely affects ATP or polyphosphate synthesis
H150Q
-
the mutation causes PPK1 protein deficient but not defective in autophosphorylation and mildly affects ATP or polyphosphate synthesis
H247A
-
38% activity compared to the wild type enzyme
H480A
-
the mutant catalytic efficiency for the polyphosphate synthesis is almost or very close to that of the wild type enzyme
H480Q
-
the mutant catalytic efficiency for the polyphosphate synthesis is almost or very close to that of the wild type enzyme
H510Q
-
the mutant catalytic efficiency for the polyphosphate synthesis is almost or very close to that of the wild type enzyme
K75A
-
89% activity compared to the wild type enzyme
N515A
-
the mutant exhibits less than 2% activity for ATP synthesis and about 65% activity for polyphosphate synthesis compared to the wild type enzyme
R431A
-
the mutant exhibits less than 5% activity for ATP synthesis and about 78% activity for polyphosphate synthesis compared to the wild type enzyme
R461A
-
the mutant exhibits less than 2% activity for ATP synthesis and about 76% activity for polyphosphate synthesis compared to the wild type enzyme
R624A
-
the mutant exhibits less than 2% activity for ATP synthesis and about 65% activity for polyphosphate synthesis compared to the wild type enzyme
R654A
-
the mutant exhibits less than 1% activity for ATP synthesis and about 90% activity for polyphosphate synthesis compared to the wild type enzyme
S668A
-
the mutant exhibits less than 5% activity for ATP synthesis and less than 30% activity for polyphosphate synthesis compared to the wild type enzyme
W129A
the proteins has significantly reduced activity as compared to wild type protein
Y524A
-
the mutant exhibits less than 10% activity for ATP synthesis and less than 20% activity for polyphosphate synthesis compared to the wild type enzyme
F125A
-
the proteins has significantly reduced activity as compared to wild type protein
-
G72A
-
the activity of MBP-G72APPK-2 and wild type proteins are similar
-
W129A
-
the proteins has significantly reduced activity as compared to wild type protein
-
F125A
-
the proteins has significantly reduced activity as compared to wild type protein
-
F67A
-
84% activity compared to the wild type enzyme
-
G69R
-
67.1% activity compared to the wild type enzyme
-
G72A
-
the activity of MBP-G72APPK-2 and wild type proteins are similar
-
H115A
-
49% activity compared to the wild type enzyme
-
H247A
-
38% activity compared to the wild type enzyme
-
K75A
-
89% activity compared to the wild type enzyme
-
W129A
-
the proteins has significantly reduced activity as compared to wild type protein
-
D395A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
F176A
-
site-directed mutagenesis, highly reduced forward and reverse reaction activities compared to the wild-type enzyme
F176Y
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
G347A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
H491A
-
site-directed mutagenesis, reduced forward and reverse reaction activities compared to the wild-type enzyme
H491A/H510A
-
site-directed mutagenesis, highly reduced forward and reverse reaction activities compared to the wild-type enzyme
H510A
-
site-directed mutagenesis, reduced forward and reverse reaction activities compared to the wild-type enzyme
L234A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
P225A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
R230A
-
site-directed mutagenesis, highly reduced forward and reverse reaction activities compared to the wild-type enzyme
R230K
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
R309A
-
site-directed mutagenesis, reduced forward and reverse reaction activities compared to the wild-type enzyme
G347A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
-
H510A
-
site-directed mutagenesis, reduced forward and reverse reaction activities compared to the wild-type enzyme
-
R230K
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
-
G347A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
-
H510A
-
site-directed mutagenesis, reduced forward and reverse reaction activities compared to the wild-type enzyme
-
R230K
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
-
D307A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D320A
-
the mutant shows reduced activity compared to the wild type enzyme
D323A
-
the mutant shows reduced activity compared to the wild type enzyme
D362A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D437A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
E304A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K311A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K473A
-
the mutant shows reduced activity compared to the wild type enzyme
Q416A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R316A
-
the mutant shows reduced activity compared to the wild type enzyme
R325A
-
the mutant shows reduced activity compared to the wild type enzyme
R363A
-
the mutant shows almost no activity compared to the wild type enzyme
R419A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R423A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R477A
-
the mutant shows increased activity compared to the wild type enzyme
W408A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
Y447A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
A106E
mutant enzyme does not show any detectable activity
A106E/H102K
mutant enzyme does not show any detectable activity
A106E/V115T
mutant enzyme does not show any detectable activity
D148A
the mutant shows strongly reduced activity compared to the wild type enzyme
D223A
the mutant shows strongly reduced activity compared to the wild type enzyme
D93A
the mutant shows strongly reduced activity compared to the wild type enzyme
E90A
the mutant shows strongly reduced activity compared to the wild type enzyme
H102K
mutant enzyme does not show any detectable activity
H102K/A106E/V115T
mutant enzyme H102K/A106E/V115T exhibits the capability to utilize polyP(4) as phosphate donor to synthesize ATP. The wild-type enzyme can not adopt polyphosphate(4)
K97A
the mutant shows strongly reduced activity compared to the wild type enzyme
Q202A
the mutant shows strongly reduced activity compared to the wild type enzyme
R149A
the mutant shows strongly reduced activity compared to the wild type enzyme
R205A
the mutant shows strongly reduced activity compared to the wild type enzyme
R209A
the mutant shows strongly reduced activity compared to the wild type enzyme
R263A
the mutant shows almost wild type activity
V115T
mutant enzyme does not show any detectable activity
V115T/H102K
mutant enzyme does not show any detectable activity
W194A
the mutant shows strongly reduced activity compared to the wild type enzyme
Y233A
the mutant shows strongly reduced activity compared to the wild type enzyme
D117N
about 300fold decrease in activity
D117N
catalytic efficiency (kcat/Km) is 5.7fold higher than wild-type value
D192A
about 10000fold decrease in activity
D192A
catalytic efficiency (kcat/Km) is 12319fold lower than wild-type value
D62A
about 1000fold decrease in activity
D62A
catalytic efficiency (kcat/Km) is 900fold lower than wild-type value
K66A
about 10000fold decrease in activity
K66A
catalytic efficiency (kcat/Km) is 131590fold lower than wild-type value
R118A
about 10000fold decrease in activity
R118A
catalytic efficiency (kcat/Km) is 15649fold lower than wild-type value
R178A
about 10000fold decrease in activity
R178A
catalytic efficiency (kcat/Km) is 6095fold lower than wild-type value
D192A
-
about 10000fold decrease in activity
-
D192A
-
catalytic efficiency (kcat/Km) is 12319fold lower than wild-type value
-
K66A
-
about 10000fold decrease in activity
-
K66A
-
catalytic efficiency (kcat/Km) is 131590fold lower than wild-type value
-
N121D
7fold decrease in activity with AMP, 25fold decrease in activity with ADP
N121D
the catalytic efficiency for ADP is 6.45fold lower than the wild-type value. The catalytic efficiency for AMP is 24fold lower than the wild-type value
N121D
-
7fold decrease in activity with AMP, 25fold decrease in activity with ADP
-
N121D
-
the catalytic efficiency for ADP is 6.45fold lower than the wild-type value. The catalytic efficiency for AMP is 24fold lower than the wild-type value
-
additional information
50% of the wild type gene are deleted, mutants reveal lower level of phosphorylated products and higher suceptibility to environmental stress
additional information
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50% of the wild type gene are deleted, mutants reveal lower level of phosphorylated products and higher suceptibility to environmental stress
additional information
generation of a targeted ppk1 deletion mutant in Campylobacter jejuni strain 81-176, which exhibits low levels of polyphosphate at all growth stages in contrast to the wild-type enzyme. The DELTAppk1 mutant is defective for survival during osmotic shock and low-nutrient stress, phenotype, overview
additional information
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generation of a targeted ppk1 deletion mutant in Campylobacter jejuni strain 81-176, which exhibits low levels of polyphosphate at all growth stages in contrast to the wild-type enzyme. The DELTAppk1 mutant is defective for survival during osmotic shock and low-nutrient stress, phenotype, overview
additional information
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50% of the wild type gene are deleted, mutants reveal lower level of phosphorylated products and higher suceptibility to environmental stress
-
additional information
-
generation of a targeted ppk1 deletion mutant in Campylobacter jejuni strain 81-176, which exhibits low levels of polyphosphate at all growth stages in contrast to the wild-type enzyme. The DELTAppk1 mutant is defective for survival during osmotic shock and low-nutrient stress, phenotype, overview
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additional information
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ppk2A and ppk2b knockout organisms, ppk2b has PPK activity
additional information
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deletion of ppk2B decreases PPK activity and cellular polyphosphate content, while overexpression of ppk2B increases both PPK activity and cellular polyphosphate content. Neither deletion nor overexpression of ppk2A changes specific activity of PPK or cellular polyphosphate content significantly. The ppk2B deletion mutant, which accumulated very little polyphopshate and grows like the wild-type under phosphate-sufficient conditions, shows a growth defect under phosphate-limiting conditions, phenotype, overview
additional information
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ppk2A and ppk2b knockout organisms, ppk2b has PPK activity
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additional information
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deletion of ppk2B decreases PPK activity and cellular polyphosphate content, while overexpression of ppk2B increases both PPK activity and cellular polyphosphate content. Neither deletion nor overexpression of ppk2A changes specific activity of PPK or cellular polyphosphate content significantly. The ppk2B deletion mutant, which accumulated very little polyphopshate and grows like the wild-type under phosphate-sufficient conditions, shows a growth defect under phosphate-limiting conditions, phenotype, overview
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additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
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construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
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additional information
DdPPK1 mutants show reduced polyphosphate levels and are defective in fruiting body development, sporulation, and predation, and in late stages of cytokinesis and cell division, overview. The enzyme-defective mutants do not produce polyphosphate exopolymer
additional information
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DdPPK1 mutants show reduced polyphosphate levels and are defective in fruiting body development, sporulation, and predation, and in late stages of cytokinesis and cell division, overview. The enzyme-defective mutants do not produce polyphosphate exopolymer
additional information
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generation of a ppk knockout mutant strain, DELTAppk
additional information
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generation of a ppk knockout mutant strain, DELTAppk
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additional information
construction of a DELTA FTT1564 enzyme gene deletion mutant strain
additional information
construction of a ppk null mutant and the ppk-complemented strain, DELTAppk and DELTAppk (pHT304-ppk)
additional information
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construction of a ppk null mutant and the ppk-complemented strain, DELTAppk and DELTAppk (pHT304-ppk)
additional information
downregulation of ppk1 leads to impaired survival of Mycobacterium tuberculosis in macrophages, the stringent response regulator ppGpp is impaired in the ppk1 knockout mutant and is restored after complementation with ppk1 of Mycobacterium tuberculosis, overview
additional information
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downregulation of ppk1 leads to impaired survival of Mycobacterium tuberculosis in macrophages, the stringent response regulator ppGpp is impaired in the ppk1 knockout mutant and is restored after complementation with ppk1 of Mycobacterium tuberculosis, overview
additional information
the ppk1 promoter of Mycobacterium tuberculosis is activated under phosphate starvation. This is attenuated upon deletion of an imperfect palindrome likely representing a binding site for the response regulator RegX3, a component of the two-component system SenX3-RegX3 that responds to phosphate starvation. The activity of the ppk1 promoter is abrogated upon deletion of a putative SigE binding site
additional information
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the ppk1 promoter of Mycobacterium tuberculosis is activated under phosphate starvation. This is attenuated upon deletion of an imperfect palindrome likely representing a binding site for the response regulator RegX3, a component of the two-component system SenX3-RegX3 that responds to phosphate starvation. The activity of the ppk1 promoter is abrogated upon deletion of a putative SigE binding site
additional information
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the ppk1 promoter of Mycobacterium tuberculosis is activated under phosphate starvation. This is attenuated upon deletion of an imperfect palindrome likely representing a binding site for the response regulator RegX3, a component of the two-component system SenX3-RegX3 that responds to phosphate starvation. The activity of the ppk1 promoter is abrogated upon deletion of a putative SigE binding site
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additional information
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downregulation of ppk1 leads to impaired survival of Mycobacterium tuberculosis in macrophages, the stringent response regulator ppGpp is impaired in the ppk1 knockout mutant and is restored after complementation with ppk1 of Mycobacterium tuberculosis, overview
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additional information
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PPK knockout organism is susceptible to oxidative stress
additional information
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effect of oxidative and surface stress as well as anaerobiosis on the survival of a ppk1 knockout mutant PPK-KO, overview. Effect of inactivation of ppk1 on the transcription of mprA, mprB, sigE and rel, overview
additional information
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PPK knockout organism is susceptible to oxidative stress
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additional information
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effect of oxidative and surface stress as well as anaerobiosis on the survival of a ppk1 knockout mutant PPK-KO, overview. Effect of inactivation of ppk1 on the transcription of mprA, mprB, sigE and rel, overview
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additional information
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PPK knockout organism is susceptible to oxidative stress
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additional information
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effect of oxidative and surface stress as well as anaerobiosis on the survival of a ppk1 knockout mutant PPK-KO, overview. Effect of inactivation of ppk1 on the transcription of mprA, mprB, sigE and rel, overview
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additional information
construction of a ppk gene encoding the PPK insertional mutant in Proteus mirabilis strain HI4320
additional information
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construction of a ppk gene encoding the PPK insertional mutant in Proteus mirabilis strain HI4320
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additional information
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ppk1 knockout organism, PAOM5, reveals profound deficiencies in cellular functions
additional information
Q9S646
ppk1 knockout organism, PAOM5, reveals profound deficiencies in cellular functions
additional information
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the PPK1-deficient strain PAOM5, an isogenic mutant of strain PAO1, is significantly less virulent than either wild-type strain PAO1 or the complemented mutant, the loss of ocular virulence is probably due to the dysregulation of multiple genes, including those responsible for stress response, the PPK1-deficient mutant produces significantly less pyocyanin, phenotype, overview
additional information
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the ppk1 knockout mutant of Pseudomonas aeruginosa strain PAO1 exhibits multiple ultrastructural and functional defects, e.g. defects in motility, quorum sensing, biofilm formation, and virulence. It shows striking compaction of the nucleoid, distortion of the cell envelope, lack of planktonic motility and exopolymer production, and susceptibility to the beta-lactam antibiotic carbenicillin as well as desiccation, mutant cells fail to produce exopolymer, phenotype, overview
additional information
Q9S646
the ppk1 knockout mutant of Pseudomonas aeruginosa strain PAO1 exhibits multiple ultrastructural and functional defects, e.g. defects in motility, quorum sensing, biofilm formation, and virulence. It shows striking compaction of the nucleoid, distortion of the cell envelope, lack of planktonic motility and exopolymer production, and susceptibility to the beta-lactam antibiotic carbenicillin as well as desiccation, mutant cells fail to produce exopolymer, phenotype, overview
additional information
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construction of a truncated enzyme mutants comprising amino acid residues 1-314 of 506 (N-paPpx(1-314)), or residues 1-303 (N-paPpx(1-303)), or residues 315-506 (C-paPpx(315-506)) of paPpx, amplified from Pseudomonas aeruginosa wild-type strain PAO1 chromosomal DNA through PCR. Only paPpx(1-506) and N-paPpx(1-314) are enzymatically active, while C-paPpx(315-506) lacks enzymatic activity
additional information
genes ppk and ppx are adjacent to each other in the genome, a ppk-deficient mutant is more sensitive to oxidative stress than the wild-type and the ppx mutant, and shows reduced growth, phenotypes, overview