1.11.1.21: catalase-peroxidase
This is an abbreviated version!
For detailed information about catalase-peroxidase, go to the full flat file.
Word Map on EC 1.11.1.21
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1.11.1.21
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1.11.1.7
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katgs
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mycobacterium
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tuberculosis
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isoniazid
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dismutase
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ascorbate
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heme
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horseradish
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peroxidases
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guaiacol
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ferric
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myeloperoxidase
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catalases
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1.6.4.2
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lignification
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monofunctional
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lactoperoxidase
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peroxidatic
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isonicotinic
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high-spin
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inh-resistant
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isoniazid-resistant
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o-dianisidine
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pseudomallei
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antituberculosis
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soret
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catalatic
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pro-drug
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antitubercular
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medicine
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mycolic
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isoperoxidase
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monodehydroascorbate
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1.8.5.1
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low-spin
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1.10.3.1
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pyrogallol
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3-amino-1,2,4-triazole
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coniferyl
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1.14.18.1
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4.3.1.5
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synthesis
- 1.11.1.21
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1.11.1.7
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katgs
- mycobacterium
- tuberculosis
- isoniazid
- dismutase
- ascorbate
- heme
- horseradish
- peroxidases
- guaiacol
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ferric
- myeloperoxidase
- catalases
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1.6.4.2
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lignification
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monofunctional
- lactoperoxidase
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peroxidatic
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isonicotinic
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high-spin
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inh-resistant
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isoniazid-resistant
- o-dianisidine
- pseudomallei
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antituberculosis
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soret
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catalatic
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pro-drug
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antitubercular
- medicine
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mycolic
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isoperoxidase
- monodehydroascorbate
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1.8.5.1
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low-spin
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1.10.3.1
- pyrogallol
- 3-amino-1,2,4-triazole
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coniferyl
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1.14.18.1
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4.3.1.5
- synthesis
Reaction
Synonyms
AfKatG, BW16_04845, CAT, CAT-2, catalase -peroxidase KatG, catalase peroxidase, catalase-peroxidase, catalase/peroxidase, CP 2, CP01, CP02, CPX, CthediskatG, EC 1.11.1.7, FeSOD A, FvCP01, FvCP02, FVEG_10866, FVEG_12888, HCP, hemoprotein b-590, HPI, hydroperoxidase I, KatG, KatG1, KatG2, KatP, katX2, KpCP, PCP, Rv1908c
ECTree
Advanced search results
Engineering
Engineering on EC 1.11.1.21 - catalase-peroxidase
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A143Q
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
A143V
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
A290Q
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
A290Y
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
D141A
D141A/R108A
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the reaction with peroxyacetic acid is clearly slower than for mutant D141A
D141E
D141N
E242Q
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
H112A
the mutant shows 0.02% of wild type catalase activity and 2.3% of wild type peroxidase activity
H112N
the mutant shows 0.05% of wild type catalase activity and 2.3% of wild type peroxidase activity
L209D
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
L236D
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
M264A
the mutant shows 0.15% of wild type catalase activity and 160% of wild type peroxidase activity
M264L
the mutant shows 0.02% of wild type catalase activity and 140% of wild type peroxidase activity
Q233E
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
R108A
R108A/D141A
R108A/W111F
the mutant shows stronglydecreased catalase and peroxidase activities
R108A/W111F/D141A
the mutant shows strongly decreased catalase and peroxidase activities
R108K
R426A
the mutant shows 4.3% of wild type catalase activity and 99% of wild type peroxidase activity
R426K
the mutant shows 70% of wild type catalase activity and 97% of wild type peroxidase activity
S324T
the mutant shows 109% of wild type catalase activity and 94% of wild type peroxidase activity
W111F
W309F
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
W330F
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the mutant exhibits slightly reduced catalase- and peroxidase-specific activities but a faster peroxidase turnover rate compared to the wild type enzyme
Y238A
the mutant shows 0.05% of wild type catalase activity and 140% of wild type peroxidase activity
Y238F
the mutant shows 0.15% of wild type catalase activity and 64% of wild type peroxidase activity
A143Q
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the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
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A143V
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the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
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D141A
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the mutant shows reduced catalase and peroxidase activities compared to the wild type enzyme
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E242Q
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the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
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W309F
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the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
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DELTA200-214
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mutation eliminates catalase activity, but variant is substantially more active as peroxidase
DELTAL193-N228
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mutant lacking Large Loop1, mutation eliminates catalase activity, but variant is substantially more active as peroxidase
H106C
H106Y
H257Y
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the mutant shows 0.05% of wild type catalase activity and 1.8% of wild type peroxidase activity
H267Y
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the peroxidatic-to-catalatic ratio of the mutant is increased 36fold, the heme content of the mutant is reduced relative to the wild type enzyme
R102C
R102K
R102L
W105F
W105L
Y111A
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the mutation leads to a 5fold reduction in the apparent kcat for catalase activity and an 8fold decrease in the apparent second-order rate constant. For peroxidase activity, the H2O2- and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)-dependent peroxidatic apparent kcat are reduced by 66% and 40%, respectively. Preparations of this variant yield a mixture of high- and low-spin heme states, thus creating the appearance of a transition between wild type (high-spin) and C-terminal lacking (low-spin) KatG
Y226F
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mutation eliminates catalase activity, but variant is substantially more active as peroxidase
H106Y
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the peroxidatic-to-catalatic ratio of the mutant is increased 321fold, the heme content of the mutant is reduced relative to the wild type enzyme
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R102C
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the peroxidatic-to-catalatic ratio of the mutant is increased 18fold, the heme content of the mutant is reduced relative to the wild type enzyme
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R102K
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the peroxidatic-to-catalatic ratio of the mutant is increased 7fold, the heme content of the mutant is reduced relative to the wild type enzyme
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R102L
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the peroxidatic-to-catalatic ratio of the mutant is increased 13fold, the heme content of the mutant is reduced relative to the wild type enzyme
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W105F
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the peroxidatic-to-catalatic ratio of the mutant is increased 2800fold, the heme content of the mutant is reduced relative to the wild type enzyme
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A110V
A139P
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site-directed mutagenesis, 76% decreased activity with and activation of isoniazid compared to the wild-type enzyme
A350T
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the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
D137S
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in the presence of H2O2, the adduct radical formed from covalently linked side chains of conserved amino acids Met255, Tyr229, and Trp107 is formed normally, but mutant is defective in forming dioxyheme and lacks catalase activity. Mutant exhibits a coincidence between adduct radical persistence and H2O2 consumption as a function of time, and enhanced subunit oligomerization during turnover
D387G
naturally occuring mutation in KatG which causes INH resistance to a very high level
D735A
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site-directed mutagenesis, 73% decreased activity with and activation of isoniazid compared to the wild-type enzyme
E291A
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the mutant shows 89% peroxidase activity and 139% catalase activity compared to the wild type enzyme
E291K
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the mutant shows 200% peroxidase activity and 79% catalase activity compared to the wild type enzyme
E291K/E292A
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the mutant shows 222% peroxidase activity and 102% catalase activity compared to the wild type enzyme
E695A
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only subtle variations in spectroscopic and catalytic properties of the enzyme, substantial decrease in the rate and extent of KatG N-terminal domain reactivation
E695A/Y697A
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substantial increase in hexa-coordinate low-spin heme and diminished enzyme activity, complete loss of the capacity for the reactivation of the N-terminal domain
G273C
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
G316S
naturally occuring mutation in KatG which does not cause INH resistance
G421S
site-directed mutagenesis, of amino acids alteration in the mutant, substitution of T354I and G421S create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis
H108L
H108Q
H97R/L200Q
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
I290A
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the mutant shows 31% peroxidase activity and 93% catalase activity compared to the wild type enzyme
I290A/Q293A
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the mutant shows 56% peroxidase activity and 64% catalase activity compared to the wild type enzyme
I290V
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the mutant shows 35% peroxidase activity and 67% catalase activity compared to the wild type enzyme
I290V/Q293V
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the mutant shows 44% peroxidase activity and 47% catalase activity compared to the wild type enzyme
L499M
naturally occuring mutation in KatG which does not cause INH resistance
L587M
L587P
naturally occuring mutation in KatG which does not cause INH resistance
L619P
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site-directed mutagenesis, no remaining activity with and activation of isoniazid
L634F
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site-directed mutagenesis, 36% decreased activity with and activation of isoniazid compared to the wild-type enzyme
L690A/R691A
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substantial increase in hexa-coordinate low-spin heme and diminished enzyme activity, complete loss of the capacity for the reactivation of the N-terminal domain
L690A/R691A/E695A/Y697A
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substantial increase in hexa-coordinate low-spin heme and diminished enzyme activity, complete loss of the capacity for the reactivation of the N-terminal domain
M255A
the mutant exhibits severely reduced catalase activity compared to the wild type enzyme
N138S
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the KatG level of the mutant is 30% of wild type level, the mutant shows a 90% reduction in peroxidase activity
N238S
the catalytic efficiency (Kcat/KM) of the mutant decreases to 41 and 52% for catalase and peroxidase, respectively, compared to the wild type enzyme
Q293A
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the mutant shows 59% peroxidase activity and 102% catalase activity compared to the wild type enzyme
Q293E
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the mutant shows 62% peroxidase activity and 80% catalase activity compared to the wild type enzyme
Q293V
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the mutant shows 25% peroxidase activity and 44% catalase activity compared to the wild type enzyme
R104L
R385W
naturally occuring mutation in KatG which causes INH resistance to a very high level
R418L
R463G
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the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
R463L
R691A
-
only subtle variations in spectroscopic and catalytic properties of the enzyme, substantial decrease in the rate and extent of KatG N-terminal domain reactivation
S140N
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
S140N/A350T/R463L/R463G/L587M
the mutant katG has catalase-peroxidase activities higher than wild-type katG and exhibits INH sensitivity
S315G
S315I
S315N
S315R
S315T
T275P
T354I
site-directed mutagenesis, of amino acids alteration in the mutant, substitution of T354I and G421S create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis
T354I/G421S/R463L/V721M
naturally occuring mutation. The Mycobacterium tubeculsosis clinical isolate R2 contains four mutations, i.e. C1061T, G1261A, G1388T, G2161A, which correspond to the amino acid substitutions T354I, G421S, R463L, and V721M, respectively, leading to high level isoniazid (INH) resistance. The mutant enzyme showed 86.5% of catalase and 45% of peroxidase activities in comparison to the wild-type enzyme. Substitutions of T354I and G421S in mutant katG R2 create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis. Mutant phenotype and stability, overview
W107F
W107F/W321F
-
the mutant shows decreased catalase catalytic efficiency compared to the wild type enzyme
W107R
site-directed mutagenesis of the catalytic residue, the mutant displays only one heme bound per homodimer of protein. The heme is absent from protomer A and displays significant structural disorder in the vicinity of the heme binding site. Several areas surrounding the heme pocket are difficult to model in protomer A, either displaying minimal or fragmented density. The mutant C-terminal domain of both protomers remains similar to wild-type KatG. The mutant's Arg residue results in disruption of the covalently linked catalytic triad. The loop containing Tyr229, which is part of the MYW catalytic triad is disordered in both protomers, presumably as a consequence of the mutation
W321F
W321G
-
the KatG level of the mutant is 40% of wild type level, the mutant shows a 70% reduction in peroxidase and catalase activities
Y229F
Y697A
-
only subtle variations in spectroscopic and catalytic properties of the enzyme, substantial decrease in the rate and extent of KatG N-terminal domain reactivation
A110V
-
naturally occuring mutation in KatG which does not cause INH resistance
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G421S
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site-directed mutagenesis, of amino acids alteration in the mutant, substitution of T354I and G421S create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis
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S140N/A350T/R463L/R463G/L587M
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the mutant katG has catalase-peroxidase activities higher than wild-type katG and exhibits INH sensitivity
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S315G
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site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
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S315I
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site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
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S315N
S315R
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site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
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S315T
T275P
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site-directed mutagenesis of the residue from the loop close to the heme binding site. The structure of mutant T275P displays significant areas of disorder compared with the wild-type KatG. Several loops surrounding the heme pocket contain little or no density in either protomer A or B. These disordered regions are identical to those in protomer A of the W107R variant. The loop containing the Thr275 residue (residues 274-329) displays no density and therefore cannot be modeled
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T354I/G421S/R463L/V721M
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naturally occuring mutation. The Mycobacterium tubeculsosis clinical isolate R2 contains four mutations, i.e. C1061T, G1261A, G1388T, G2161A, which correspond to the amino acid substitutions T354I, G421S, R463L, and V721M, respectively, leading to high level isoniazid (INH) resistance. The mutant enzyme showed 86.5% of catalase and 45% of peroxidase activities in comparison to the wild-type enzyme. Substitutions of T354I and G421S in mutant katG R2 create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis. Mutant phenotype and stability, overview
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W107R
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site-directed mutagenesis of the catalytic residue, the mutant displays only one heme bound per homodimer of protein. The heme is absent from protomer A and displays significant structural disorder in the vicinity of the heme binding site. Several areas surrounding the heme pocket are difficult to model in protomer A, either displaying minimal or fragmented density. The mutant C-terminal domain of both protomers remains similar to wild-type KatG. The mutant's Arg residue results in disruption of the covalently linked catalytic triad. The loop containing Tyr229, which is part of the MYW catalytic triad is disordered in both protomers, presumably as a consequence of the mutation
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A110V
-
naturally occuring mutation in KatG which does not cause INH resistance
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G421S
-
site-directed mutagenesis, of amino acids alteration in the mutant, substitution of T354I and G421S create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis
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L587M
-
the mutant has wild type-like strong catalase and peroxidase activities
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M255A
-
the mutant exhibits severely reduced catalase activity compared to the wild type enzyme
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N238S
-
the catalytic efficiency (Kcat/KM) of the mutant decreases to 41 and 52% for catalase and peroxidase, respectively, compared to the wild type enzyme
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R104L
R418L
-
the mutant shows 0.6% of wild type catalase activity and 192% of wild type peroxidase activity
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R463L
S140N
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
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S140N/A350T/R463L/R463G/L587M
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the mutant katG has catalase-peroxidase activities higher than wild-type katG and exhibits INH sensitivity
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S315G
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
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S315I
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site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
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S315N
S315R
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site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
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S315T
T275P
T354I/G421S/R463L/V721M
-
naturally occuring mutation. The Mycobacterium tubeculsosis clinical isolate R2 contains four mutations, i.e. C1061T, G1261A, G1388T, G2161A, which correspond to the amino acid substitutions T354I, G421S, R463L, and V721M, respectively, leading to high level isoniazid (INH) resistance. The mutant enzyme showed 86.5% of catalase and 45% of peroxidase activities in comparison to the wild-type enzyme. Substitutions of T354I and G421S in mutant katG R2 create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis. Mutant phenotype and stability, overview
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W107F
-
the mutant exhibits severely reduced catalase activity yet normal peroxidase activity and contains more abundant 6-coordinate heme in high spin and low spin forms compared to the wild type enzyme
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W107R
-
site-directed mutagenesis of the catalytic residue, the mutant displays only one heme bound per homodimer of protein. The heme is absent from protomer A and displays significant structural disorder in the vicinity of the heme binding site. Several areas surrounding the heme pocket are difficult to model in protomer A, either displaying minimal or fragmented density. The mutant C-terminal domain of both protomers remains similar to wild-type KatG. The mutant's Arg residue results in disruption of the covalently linked catalytic triad. The loop containing Tyr229, which is part of the MYW catalytic triad is disordered in both protomers, presumably as a consequence of the mutation
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W321F
-
the mutant shows 38% of wild type catalase activity and 18% of wild type peroxidase activity
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Y229F
C26A/C74A
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
C55A
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
C55A/C74A
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
C74A
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
R461A
C26A/C74A
Pyricularia grisea ATCC MYA-4617
-
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
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C55A
Pyricularia grisea ATCC MYA-4617
-
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
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C55A/C74A
Pyricularia grisea ATCC MYA-4617
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kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
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C74A
Pyricularia grisea ATCC MYA-4617
-
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
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S308T
D152N
the mutant shows 2.7% of wild type catalase activity and 234% of wild type peroxidase activity
D152S
the mutant shows 5.7% of wild type catalase activity and 237% of wild type peroxidase activity
D152W
the mutant shows 0.6% of wild type catalase activity and 672% of wild type peroxidase activity
D402E
the mutant shows 0.6% of wild type catalase activity and 65% of wild type peroxidase activity
D402N
the mutant shows 0.5% of wild type catalase activity and 56% of wild type peroxidase activity
E253D
the mutant shows 42% of wild type catalase activity and 280% of wild type peroxidase activity
E253Q
the mutant shows 25% of wild type catalase activity and 96% of wild type peroxidase activity
H123E
the mutant shows 0.03% of wild type catalase activity and 13% of wild type peroxidase activity
H123Q
the mutant shows 0.02% of wild type catalase activity and 7.4% of wild type peroxidase activity
H290Q
the mutant shows 0.09% of wild type catalase activity and 5.6% of wild type peroxidase activity
I248F
the mutant shows 12% of wild type catalase activity and 124% of wild type peroxidase activity
M275I
the mutant shows 0.6% of wild type catalase activity and 640% of wild type peroxidase activity
N153A
the mutant shows 6% of wild type catalase activity and 60% of wild type peroxidase activity
N153D
the mutant shows 17% of wild type catalase activity and 130% of wild type peroxidase activity
N251L
the mutant shows 33% of wild type catalase activity and 415% of wild type peroxidase activity
P252A
the mutant shows 110% of wild type catalase activity and 97% of wild type peroxidase activity
R119A
the mutant shows 15% of wild type catalase activity and 12% of wild type peroxidase activity
R119N
the mutant shows 0.5% of wild type catalase activity and 5% of wild type peroxidase activity
R439A
the mutant shows 4.9% of wild type catalase activity and 12% of wild type peroxidase activity
R439N
the mutant shows 3.1% of wild type catalase activity and 100% wild type peroxidase activity
S335T
the mutant shows 99% of wild type catalase activity and 103% of wild type peroxidase activity
W122A
the mutant shows no catalase activity and 100% wild type peroxidase activity
W122F
the mutant shows no catalase activity and 90% of wild type peroxidase activity
W341A
the mutant shows 0.5% of wild type catalase activity and 25% of wild type peroxidase activity
W341F
the mutant shows 42% of wild type catalase activity and 190% of wild type peroxidase activity
Y249F
the mutant shows 0.17% of wild type catalase activity and 121% of wild type peroxidase activity
D152N
-
the mutant shows 2.7% of wild type catalase activity and 234% of wild type peroxidase activity
-
D402E
-
the mutant shows 0.6% of wild type catalase activity and 65% of wild type peroxidase activity
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D402N
-
the mutant shows 0.5% of wild type catalase activity and 56% of wild type peroxidase activity
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H290Q
-
the mutant shows 0.09% of wild type catalase activity and 5.6% of wild type peroxidase activity
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R119A
-
the mutant shows 15% of wild type catalase activity and 12% of wild type peroxidase activity
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D152N
-
site-directed mutagenesis, 2.7% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile
D152S
D152W
-
site-directed mutagenesis, 0.6% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile
N153A
-
the mutant shows 6% of wild type catalase activity and exhibits an overall peroxidase activity similar with wild type KatG
N153D
-
the mutant shows 16.5% of wild type catalase activity and exhibits an overall peroxidase activity similar with wild type KatG
P151A
-
site-directed mutagenesis, slightly increased catalase activity compared to the wild-type enzyme
W122F
Y249F
D152N
-
site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, reduced catalase activity and increased peroxidase activity compared to the wild-type enzyme
D152S
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site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, reduced catalase activity and increased peroxidase activity compared to the wild-type enzyme
D152W
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site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, highly reduced catalase activity and highly increased peroxidase activity compared to the wild-type enzyme
D402E
-
site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, reduced catalase and peroxidase activity compared to the wild-type enzyme
D402N
-
site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, reduced catalase and peroxidase activity compared to the wild-type enzyme
H290Q
-
site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, highly reduced catalase and peroxidase activity compared to the wild-type enzyme
N153A
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site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction
N153D
-
site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction
P151A
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site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, slightly reduced catalase and peroxidase activity compared to the wild-type enzyme
W341A
-
site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, highly reduced catalase and peroxidase activity compared to the wild-type enzyme
W341F
-
site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, 50% reduced catalase activity and 50% increased peroxidase activity compared to the wild-type enzyme, binds completely to NaF
additional information
D141A
-
the mutant lacks an aspartate at the entrance to the heme cavity. The reaction with peroxyacetic acid proceeds much faster than for the wild type enzyme
D141A
the mutant shows 1.5% of wild type catalase activity and 132% of wild type peroxidase activity
D141A
the mutant shows decreased catalase and peroxidase activities
D141A
the mutant shows reduced catalase and peroxidase activities compared to the wild type enzyme
-
mutant with normal catalase activity but with modified kinetics
D141E
the mutant retains normal catalase activity and decreased peroxidase activity
D141E
the mutant shows 80% of wild type catalase activity and 143% of wild type peroxidase activity
the mutant shows 10% of wild type catalase activity and 123% of wild type peroxidase activity
D141N
the mutant shows decreased catalase and peroxidase activities
R108A
the mutant shows 31% of wild type catalase activity and 23% of wild type peroxidase activity
R108A
the mutation causes a reduction in catalase activity to 35% of native levels and a decrease in peroxidase activity
R108A
-
the reaction with peroxyacetic acid is clearly slower than for mutant D141A
R108A/D141A
the mutant exhibits near normal catalase activity (82% of native) and decreased peroxidase activity
the mutant shows 8% of wild type catalase activity and 21% of wild type peroxidase activity
R108K
the mutant shows decreased catalase and peroxidase activities
W111F
the mutant shows 0.05% of wild type catalase activity and 75% of wild type peroxidase activity
-
the mutant shows 0.01% of wild type catalase activity and 1.7% of wild type peroxidase activity
H106C
-
the peroxidatic-to-catalatic ratio of the mutant is increased 125fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
the mutant shows 0.008% of wild type catalase activity and 2.7% of wild type peroxidase activity
H106Y
-
the peroxidatic-to-catalatic ratio of the mutant is increased 321fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
the mutant shows 0.5% of wild type catalase activity and 10% of wild type peroxidase activity
R102C
-
the peroxidatic-to-catalatic ratio of the mutant is increased 18fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
the mutant shows 1.8% of wild type catalase activity and 13% of wild type peroxidase activity
R102K
-
the peroxidatic-to-catalatic ratio of the mutant is increased 7fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
the mutant shows 1% of wild type catalase activity and 13% of wild type peroxidase activity
R102L
-
the peroxidatic-to-catalatic ratio of the mutant is increased 13fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
the mutant shows 0.1% of wild type catalase activity and 288% of wild type peroxidase activity
W105F
-
the peroxidatic-to-catalatic ratio of the mutant is increased 2800fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
the mutant shows 0.3% of wild type catalase activity and 197% of wild type peroxidase activity
W105L
-
the peroxidatic-to-catalatic ratio of the mutant is increased 612fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
site-directed mutagenesis, catalytic efficiency with and activation of isoniazid similar to the wild-type enzyme, reduced Km and increased kcat compared to the wild-type
A110V
naturally occuring mutation in KatG which does not cause INH resistance
-
the mutant has lost both peroxidatic and catalatic activities
H108L
-
the mutant shows decreased catalase catalytic efficiency compared to the wild type enzyme
the mutant shows 0.03% of wild type catalase activity and 47% of wild type peroxidase activity
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
L587M
-
the mutant has wild type-like strong catalase and peroxidase activities
R104L
the mutant shows 0.06% of wild type catalase activity and 200% of wild type peroxidase activity
the mutant shows 0.6% of wild type catalase activity and 192% of wild type peroxidase activity
R418L
-
mutant is catalase deficient but exhibits normal formation of the adduct radical formed from covalently linked side chains of conserved amino acids Met255, Tyr229, and Trp107 and dioxyheme. Mutant exhibits a coincidence between adduct radical persistence and H2O2 consumption as a function of time, and enhanced subunit oligomerization during turnover
-
isoniazid-resistant clinical mutant, which has retained peroxidatic and catalatic activities
R463L
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
R463L
-
the mutant has wild type-like strong catalase and peroxidase activities
R463L
-
the mutation is found in isoniazid-resistant strains and does not lead to a loss of peroxidase or catalase activity
R463L
naturally occuring mutation in KatG which does not cause INH resistance
S315G
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
S315G
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
S315I
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
S315I
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
site-directed mutagenesis, no remaining activity with and activation of isoniazid
S315N
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
S315N
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
S315R
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
S315R
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
most prevalent isonazid-resistant mutant, determination of Fe2+-binding/interaction structure, minimal alterations compared to the wild-type enzyme, mutant enzyme retains all active site properties for proper catalytic function
S315T
-
isoniazid-resistant, mutant catalase-peroxidase retains all active site properties for proper catalytic function
S315T
-
the KatG level of the mutant is 90% of wild type level, the mutant shows 60% peroxidase and 40% catalase activity compared to the wild type enzyme
S315T
-
the mutant has weak catalase and barely detectable peroxidase activities
S315T
-
the mutant is a competent catalase-peroxidase with reduced activity toward isoniazid. The catalase activity is reduced 6fold and the peroxidase activity is decreased less than 2fold compared with the activities for the wild type enzyme
S315T
the mutant shows 52% of wild type catalase activity and 50% of wild type peroxidase activity
S315T
naturally occuring mutant, the mutant katG retains peroxidase and catalase activity as 60% and 40%, respectively, from wild-type activity, the mutant develops INH inhibitory levels to the transformant BCG corresponding to the decline of its protein activity
S315T
naturally occuring mutation in KatG which restricts a pathway into a catalytic heme center in the active site causing INH resistance
S315T
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
S315T
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
T275P
site-directed mutagenesis of the residue from the loop close to the heme binding site. The structure of mutant T275P displays significant areas of disorder compared with the wild-type KatG. Several loops surrounding the heme pocket contain little or no density in either protomer A or B. These disordered regions are identical to those in protomer A of the W107R variant. The loop containing the Thr275 residue (residues 274-329) displays no density and therefore cannot be modeled
the mutant exhibits severely reduced catalase activity yet normal peroxidase activity and contains more abundant 6-coordinate heme in high spin and low spin forms compared to the wild type enzyme
W107F
-
the mutant shows decreased catalase catalytic efficiency compared to the wild type enzyme
the mutant shows 38% of wild type catalase activity and 18% of wild type peroxidase activity
W321F
-
the mutant shows decreased catalase catalytic efficiency compared to the wild type enzyme
the mutant exhibits severely reduced catalase activity compared to the wild type enzyme
Y229F
the mutant shows 0.002% of wild type catalase activity and 1360% of wild type peroxidase activity
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315N
-
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
-
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315T
-
naturally occuring mutant, the mutant katG retains peroxidase and catalase activity as 60% and 40%, respectively, from wild-type activity, the mutant develops INH inhibitory levels to the transformant BCG corresponding to the decline of its protein activity
-
S315T
-
naturally occuring mutation in KatG which restricts a pathway into a catalytic heme center in the active site causing INH resistance
-
S315T
-
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
-
R104L
-
the mutant shows 0.06% of wild type catalase activity and 200% of wild type peroxidase activity
-
-
the mutant has wild type-like strong catalase and peroxidase activities
-
R463L
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
-
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315N
-
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
-
-
the mutant has weak catalase and barely detectable peroxidase activities
-
S315T
-
the KatG level of the mutant is 90% of wild type level, the mutant shows 60% peroxidase and 40% catalase activity compared to the wild type enzyme
-
S315T
-
the mutant shows 52% of wild type catalase activity and 50% of wild type peroxidase activity
-
S315T
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315T
-
naturally occuring mutant, the mutant katG retains peroxidase and catalase activity as 60% and 40%, respectively, from wild-type activity, the mutant develops INH inhibitory levels to the transformant BCG corresponding to the decline of its protein activity
-
S315T
-
naturally occuring mutation in KatG which restricts a pathway into a catalytic heme center in the active site causing INH resistance
-
S315T
-
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
-
T275P
-
site-directed mutagenesis of the residue from the loop close to the heme binding site. The structure of mutant T275P displays significant areas of disorder compared with the wild-type KatG. Several loops surrounding the heme pocket contain little or no density in either protomer A or B. These disordered regions are identical to those in protomer A of the W107R variant. The loop containing the Thr275 residue (residues 274-329) displays no density and therefore cannot be modeled
-
-
the mutant exhibits severely reduced catalase activity compared to the wild type enzyme
-
Y229F
-
the mutant shows 0.002% of wild type catalase activity and 1360% of wild type peroxidase activity
-
the mutation slightly increases the thermal stability but does not alter the active site architecture or the kinetics of cyanide binding. However, the variant loses the wild type-typical optimum of catalase activity at pH 5.3 but exhibits a broad plateau between pH 4.5 and 7.5
R461A
Pyricularia grisea 70-15
-
the mutation slightly increases the thermal stability but does not alter the active site architecture or the kinetics of cyanide binding. However, the variant loses the wild type-typical optimum of catalase activity at pH 5.3 but exhibits a broad plateau between pH 4.5 and 7.5
-
the mutant shows strongly reduced activity compared to the wild type enzyme
S308T
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
-
site-directed mutagenesis, 5.7% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile
-
the bimolecular rate constants of dioxygen binding to ferrous Y249F is 1.3fold higher than the wild-type value. The dissociation constants of the ferrous-dioxygen is 1.5fold higher than wild-type value
-
the heme environment of mutant KatGDELTAFG (lacking its FG insertion) is highly similar to wild type KatG, but the variant retains only 0.2% catalase activity. In contrast, the deletion reduces peroxidase activity by only 50%
additional information
generation of single and double gene deletion mutants of genes FvCP01 and FvCP02 encoding isozyme in KatG1 and KatG2, respectively, in the maize pathogen Fusarium verticillioides. Both mutants DELTAFvCP01 and DELTAFvCP02 are more sensitive to H2O2 than the wild-type in vitro, although their sensitivity differ depending on the type of inoculum. Inoculations using mycelial agar plugs demonstrate an additive effect of the mutants, with the DELTAFvCP01/DELTAFvCP02 double deletion being the most sensitive to H2O2. In general, conidia are much more sensitive than agar plugs to H2O2, and conidial inoculations indicate that FvCP01 confers more H2O2 tolerance than FvCP02. Phenotypes, detailed overview
additional information
generation of single and double gene deletion mutants of genes FvCP01 and FvCP02 encoding isozyme in KatG1 and KatG2, respectively, in the maize pathogen Fusarium verticillioides. Both mutants DELTAFvCP01 and DELTAFvCP02 are more sensitive to H2O2 than the wild-type in vitro, although their sensitivity differ depending on the type of inoculum. Inoculations using mycelial agar plugs demonstrate an additive effect of the mutants, with the DELTAFvCP01/DELTAFvCP02 double deletion being the most sensitive to H2O2. In general, conidia are much more sensitive than agar plugs to H2O2, and conidial inoculations indicate that FvCP01 confers more H2O2 tolerance than FvCP02. Phenotypes, detailed overview
additional information
-
generation of single and double gene deletion mutants of genes FvCP01 and FvCP02 encoding isozyme in KatG1 and KatG2, respectively, in the maize pathogen Fusarium verticillioides. Both mutants DELTAFvCP01 and DELTAFvCP02 are more sensitive to H2O2 than the wild-type in vitro, although their sensitivity differ depending on the type of inoculum. Inoculations using mycelial agar plugs demonstrate an additive effect of the mutants, with the DELTAFvCP01/DELTAFvCP02 double deletion being the most sensitive to H2O2. In general, conidia are much more sensitive than agar plugs to H2O2, and conidial inoculations indicate that FvCP01 confers more H2O2 tolerance than FvCP02. Phenotypes, detailed overview
additional information
Fusarium verticillioides FGSC 7600
-
generation of single and double gene deletion mutants of genes FvCP01 and FvCP02 encoding isozyme in KatG1 and KatG2, respectively, in the maize pathogen Fusarium verticillioides. Both mutants DELTAFvCP01 and DELTAFvCP02 are more sensitive to H2O2 than the wild-type in vitro, although their sensitivity differ depending on the type of inoculum. Inoculations using mycelial agar plugs demonstrate an additive effect of the mutants, with the DELTAFvCP01/DELTAFvCP02 double deletion being the most sensitive to H2O2. In general, conidia are much more sensitive than agar plugs to H2O2, and conidial inoculations indicate that FvCP01 confers more H2O2 tolerance than FvCP02. Phenotypes, detailed overview
-
additional information
-
generation of single and double gene deletion mutants of genes FvCP01 and FvCP02 encoding isozyme in KatG1 and KatG2, respectively, in the maize pathogen Fusarium verticillioides. Both mutants DELTAFvCP01 and DELTAFvCP02 are more sensitive to H2O2 than the wild-type in vitro, although their sensitivity differ depending on the type of inoculum. Inoculations using mycelial agar plugs demonstrate an additive effect of the mutants, with the DELTAFvCP01/DELTAFvCP02 double deletion being the most sensitive to H2O2. In general, conidia are much more sensitive than agar plugs to H2O2, and conidial inoculations indicate that FvCP01 confers more H2O2 tolerance than FvCP02. Phenotypes, detailed overview
-
additional information
dynamic simulations of enzyme mutants bound to isoniazid (INH)
additional information
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dynamic simulations of enzyme mutants bound to isoniazid (INH)
additional information
enzyme mutants' tertiary structures analysis, detailed overview
additional information
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enzyme mutants' tertiary structures analysis, detailed overview
additional information
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dynamic simulations of enzyme mutants bound to isoniazid (INH)
-
additional information
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enzyme mutants' tertiary structures analysis, detailed overview
-
additional information
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dynamic simulations of enzyme mutants bound to isoniazid (INH)
-
additional information
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enzyme mutants' tertiary structures analysis, detailed overview
-