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Information on EC 1.11.1.21 - catalase-peroxidase and Organism(s) Burkholderia pseudomallei and UniProt Accession Q939D2
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1.11.1.21 catalase-peroxidaseIUBMB Comments
Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with H2O2 as donor, releasing O2; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.
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Word Map
- 1.11.1.21
-
1.11.1.7
-
katgs
- mycobacterium
- tuberculosis
- isoniazid
- dismutase
- ascorbate
- heme
- horseradish
- peroxidases
- guaiacol
-
ferric
- myeloperoxidase
- catalases
-
1.6.4.2
-
lignification
-
monofunctional
- lactoperoxidase
-
peroxidatic
-
isonicotinic
-
high-spin
-
inh-resistant
-
isoniazid-resistant
- o-dianisidine
- pseudomallei
-
antituberculosis
-
soret
-
catalatic
-
pro-drug
-
antitubercular
- medicine
-
mycolic
-
isoperoxidase
- monodehydroascorbate
-
1.8.5.1
-
low-spin
-
1.10.3.1
- pyrogallol
- 3-amino-1,2,4-triazole
-
coniferyl
-
1.14.18.1
-
4.3.1.5
- synthesis
The taxonomic range for the selected organisms is: Burkholderia pseudomallei
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
catalase-peroxidase, catalase peroxidase, catalase/peroxidase, hydroperoxidase i, katg2, katx2, katg1, fvcp02, fvcp01, afkatg, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
KatG
KatG
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 H2O2 = O2 + 2 H2O
the catalytically relevant active site residues Trp111, Tyr238, and Met264 are linked by a covalent structure
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
donor:hydrogen-peroxide oxidoreductase
Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with H2O2 as donor, releasing O2; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
H2O2
O2 + H2O
detoxification enzyme, protection against peroxides
-
-
?
H2O2
O2 + H2O
-
it is proposed that binding of substrate H2O2 to Asp141 and Arg108 controls H2O2 access to the heme active site, thereby modulating the catalase reaction
-
-
?
peroxyacetic acid
?
-
-
in the absence of peroxidatic one-electron donors, the ferryl intermediates generated with a low excess of peroxyacetic acid slowly decay to the ferric resting state after several minutes. The Fe(IV)=O Trp330 radical cation, Fe(IV)=O Trp139 radical, and Fe(IV)=O Trp153 radical intermediates of the peroxidase-like cycle, formed with a low excess of peroxyacetic acid at low temperature, are also generated with a high excess of peroxyacetic acid at room temperature. Under high excess conditions, there is a rapid conversion to a persistent Fe(IV)=O intermediate. Specific tryptophan residues including W330, W139, and W153, methionine residues including Met264 of the M-Y-W adduct, and cysteine residues are either modified with one, two, or three oxygen atoms or cannot be identified in the spectrum because of other undetermined modifications. These oxidized residues are the source of electrons used to reduce the excess of peroxyacetic acid to acetic acid and return the enzyme to the ferric state
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
H2O2
O2 + H2O
detoxification enzyme, protection against peroxides
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
it is proposed that binding of substrate H2O2 to Asp141 and Arg108 controls H2O2 access to the heme active site, thereby modulating the catalase reaction
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
enzyme contains a heme modified with a special hydroperoxide group added to ring I
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.5 and 25°C
0.0055
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
mutant enzyme R108A/W111F/D141A, peroxidase activity, at pH 4.5 and 25°C
0.0092
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
mutant enzyme D141N, peroxidase activity, at pH 4.5 and 25°C
0.024
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
mutant enzyme R108A/W111F, peroxidase activity, at pH 4.5 and 25°C
0.03
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
mutant enzyme D141A, peroxidase activity, at pH 4.5 and 25°C
0.07
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
mutant enzyme D141E, peroxidase activity, at pH 4.5 and 25°C
0.07
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
mutant enzyme R108A/D141A, peroxidase activity, at pH 4.5 and 25°C
0.14
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
wild type enzyme, peroxidase activity, at pH 4.5 and 25°C
0.41
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
mutant enzyme R108A, peroxidase activity, at pH 4.5 and 25°C
0.55
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
mutant enzyme R108K, peroxidase activity, at pH 4.5 and 25°C
0.09
H2O2
mutant enzyme D141N, peroxidase activity, at pH 4.5 and 25°C
0.12
H2O2
mutant enzyme D141E, peroxidase activity, at pH 4.5 and 25°C
0.19
H2O2
mutant enzyme D141A, peroxidase activity, at pH 4.5 and 25°C
0.27
H2O2
mutant enzyme R108A/D141A, peroxidase activity, at pH 4.5 and 25°C
0.31
H2O2
wild type enzyme, peroxidase activity, at pH 4.5 and 25°C
0.5
H2O2
mutant enzyme R108A, peroxidase activity, at pH 4.5 and 25°C
0.56
H2O2
mutant enzyme R108A/W111F, peroxidase activity, at pH 4.5 and 25°C
0.92
H2O2
mutant enzyme R108A/W111F/D141A, peroxidase activity, at pH 4.5 and 25°C
0.98
H2O2
mutant enzyme R108K, peroxidase activity, at pH 4.5 and 25°C
3.7
H2O2
wild type enzyme, catalase activity, at pH 7.0 and 37°C
13
H2O2
mutant enzyme R108A, catalase activity, at pH 7.0 and 37°C
32
H2O2
mutant enzyme R108A/D141A, catalase activity, at pH 7.0 and 37°C
35
H2O2
mutant enzyme R108A/W111F/D141A, catalase activity, at pH 7.0 and 37°C
36
H2O2
mutant enzyme R108A/W111F, catalase activity, at pH 7.0 and 37°C
60
H2O2
mutant enzyme D141A, catalase activity, at pH 7.0 and 37°C
75
H2O2
mutant enzyme D141E, catalase activity, at pH 7.0 and 37°C
95
H2O2
mutant enzyme D141N, catalase activity, at pH 7.0 and 37°C
180
H2O2
mutant enzyme R108K, catalase activity, at pH 7.0 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.9
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.5 and 25°C
0.22
H2O2
mutant enzyme R108A/W111F, peroxidase activity, at pH 4.5 and 25°C
0.29
H2O2
mutant enzyme R108A/W111F/D141A, peroxidase activity, at pH 4.5 and 25°C
3.8
H2O2
mutant enzyme R108K, peroxidase activity, at pH 4.5 and 25°C
5.9
H2O2
mutant enzyme R108A/D141A, peroxidase activity, at pH 4.5 and 25°C
7.3
H2O2
mutant enzyme D141E, peroxidase activity, at pH 4.5 and 25°C
8.2
H2O2
mutant enzyme D141A, peroxidase activity, at pH 4.5 and 25°C
8.2
H2O2
mutant enzyme R108A, peroxidase activity, at pH 4.5 and 25°C
9.8
H2O2
mutant enzyme D141N, peroxidase activity, at pH 4.5 and 25°C
14.4
H2O2
wild type enzyme, peroxidase activity, at pH 4.5 and 25°C
32
H2O2
mutant enzyme R108A/W111F/D141A, catalase activity, at pH 7.0 and 37°C
34
H2O2
mutant enzyme R108A/W111F, catalase activity, at pH 7.0 and 37°C
265
H2O2
mutant enzyme D141A, catalase activity, at pH 7.0 and 37°C
1190
H2O2
mutant enzyme D141N, catalase activity, at pH 7.0 and 37°C
1950
H2O2
mutant enzyme R108A, catalase activity, at pH 7.0 and 37°C
2110
H2O2
mutant enzyme R108K, catalase activity, at pH 7.0 and 37°C
4620
H2O2
mutant enzyme R108A/D141A, catalase activity, at pH 7.0 and 37°C
5680
H2O2
wild type enzyme, catalase activity, at pH 7.0 and 37°C
6140
H2O2
mutant enzyme D141E, catalase activity, at pH 7.0 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.32
H2O2
mutant enzyme R108A/W111F/D141A, peroxidase activity, at pH 4.5 and 25°C
0.39
H2O2
mutant enzyme R108A/W111F, peroxidase activity, at pH 4.5 and 25°C
0.9
H2O2
mutant enzyme R108A/W111F, catalase activity, at pH 7.0 and 37°C
0.9
H2O2
mutant enzyme R108A/W111F/D141A, catalase activity, at pH 7.0 and 37°C
1.3
H2O2
mutant enzyme D141N, catalase activity, at pH 7.0 and 37°C
3.9
H2O2
mutant enzyme R108K, peroxidase activity, at pH 4.5 and 25°C
4.4
H2O2
mutant enzyme D141A, catalase activity, at pH 7.0 and 37°C
8.2
H2O2
mutant enzyme D141E, catalase activity, at pH 7.0 and 37°C
12
H2O2
mutant enzyme R108K, catalase activity, at pH 7.0 and 37°C
16
H2O2
mutant enzyme R108A, peroxidase activity, at pH 4.5 and 25°C
22
H2O2
mutant enzyme R108A/D141A, peroxidase activity, at pH 4.5 and 25°C
43
H2O2
mutant enzyme D141A, peroxidase activity, at pH 4.5 and 25°C
46
H2O2
wild type enzyme, peroxidase activity, at pH 4.5 and 25°C
61
H2O2
mutant enzyme D141E, peroxidase activity, at pH 4.5 and 25°C
110
H2O2
mutant enzyme D141N, peroxidase activity, at pH 4.5 and 25°C
140
H2O2
mutant enzyme R108A/D141A, catalase activity, at pH 7.0 and 37°C
150
H2O2
mutant enzyme R108A, catalase activity, at pH 7.0 and 37°C
1500
H2O2
wild type enzyme, catalase activity, at pH 7.0 and 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2200
purified recombinant enzyme, catalase-specific activity
4.8
-
peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 4.5 and 25°C
5.3
-
peroxidase specific activity, using o-dianisidine as substrate, at pH 4.5 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene katG, bifunctional enzyme KatG with catalase and peroxidase activities
SwissProt
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
active site structure analysis of wild-type and mutant W111F enzymes
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 16-20% (w/v) PEG 4K, 20% (v/v) 2-methyl-2,4-pentanediol and 0.1 M sodium citrate pH 5.6, at 20°C
purified recombinant enzyme, hanging drop vapour diffusion method, 0.001 ml of 22 mg/ml protein in potassium phosphate, pH 7.0, mixed with equal volume of reservoir solution containing 16-20% PEG 4000, 20% 2-methyl-2,4-pentanediol, and 0.1 M sodium citrate, pH 5.6, 3-5 days, 20°C, X-ray diffraction strcuture determination and analysis at 1.8 A resolution, molecular replacement
crystal structure of the D141E variant determined at 1.8 A resolution
-
mutant enzyme D141A in complex with isoniazid, hanging drop vapor diffusion method, using 16-20% (w/v) PEG 4000, 20% (w/v) 2-methyl-2,4-pentanediol, and 0.1 M sodium citrate pH 5.6
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D141A
D141E
D141N
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
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
R108A
R108A/D141A
the mutant exhibits near normal catalase activity (82% of native) and decreased peroxidase activity
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
the mutant shows 0.05% of wild type catalase activity and 75% of wild type peroxidase activity
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
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
-
the reaction with peroxyacetic acid is clearly slower than for mutant D141A
D141E
-
mutant with normal catalase activity but with modified kinetics
E242Q
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
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
Q233E
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
R108A
W309F
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
W330F
-
the mutant exhibits slightly reduced catalase- and peroxidase-specific activities but a faster peroxidase turnover rate compared to 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
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
D141N
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
R108K
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
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 reduced catalase and peroxidase activities compared to the wild type enzyme
R108A
-
the reaction with peroxyacetic acid is clearly slower than for mutant D141A
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
-
the enzyme is completely inactive after less than 1 min at 65°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE-cellulose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the enzyme responsible for the activation of isoniazid as an antibiotic
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Carpena, X.; Switala, J.; Loprasert, S.; Mongkolsuk, S.; Fita, I.; Loewen, P.C.
Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomallei
Acta Crystallogr. Sect. D
58
2184-2186
2002
Burkholderia pseudomallei (Q939D2), Burkholderia pseudomallei
Donald, L.J.; Krokhin, O.V.; Duckworth, H.W.; Wiseman, B.; Deemagarn, T.; Singh, R.; Switala, J.; Carpena, X.; Fita, I.; Loewen, P.C.
Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry
J. Biol. Chem.
278
35687-35692
2003
Burkholderia pseudomallei
Deemagarn, T.; Wiseman, B.; Carpena, X.; Ivancich, A.; Fita, I.; Loewen, P.C.
Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei
Proteins
66
219-228
2007
Burkholderia pseudomallei
Singh, R.; Wiseman, B.; Deemagarn, T.; Jha, V.; Switala, J.; Loewen, P.
Comparative study of catalase-peroxidases (KatGs)
Arch. Biochem. Biophys.
471
207-214
2008
Archaeoglobus fulgidus, Burkholderia pseudomallei, Escherichia coli, Geobacillus stearothermophilus, Mycobacterium tuberculosis, Rhodobacter capsulatus, Synechocystis sp.
Vlasits, J.; Jakopitsch, C.; Bernroitner, M.; Zamocky, M.; Furtmueller, P.G.; Obinger, C.
Mechanisms of catalase activity of heme peroxidases
Arch. Biochem. Biophys.
500
74-81
2010
Haloarcula marismortui (O59651), Mycobacterium tuberculosis (P9WIE5), Synechococcus elongatus (Q31MN3), Burkholderia pseudomallei (Q939D2), Mycobacterium tuberculosis H37Rv (P9WIE5), Synechococcus elongatus PCC 7942 (Q31MN3)
Wiseman, B.; Colin, J.; Smith, A.T.; Ivancich, A.; Loewen, P.C.
Mechanistic insight into the initiation step of the reaction of Burkholderia pseudomallei catalase-peroxidase with peroxyacetic acid
J. Biol. Inorg. Chem.
14
801-811
2009
Burkholderia pseudomallei
Smulevich, G.; Jakopitsch, C.; Droghetti, E.; Obinger, C.
Probing the structure and bifunctionality of catalase-peroxidase (KatG)
J. Inorg. Biochem.
100
568-585
2006
Escherichia coli, Mycobacterium tuberculosis (P9WIE5), Synechococcus sp. (Q31MN3), Burkholderia pseudomallei (Q939D2), Synechococcus sp. PCC 7942 (Q31MN3), Mycobacterium tuberculosis H37Rv (P9WIE5)
Carpena, X.; Loprasert, S.; Mongkolsuk, S.; Switala, J.; Loewen, P.C.; Fita, I.
Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution
J. Mol. Biol.
327
475-489
2003
Burkholderia pseudomallei (Q939D2), Burkholderia pseudomallei
Deemagarn, T.; Wiseman, B.; Carpena, X.; Ivancich, A.; Fita, I.; Loewen, P.C.
Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei
Proteins Struct. Funct. Bioinform.
66
219-228
2007
Burkholderia pseudomallei (Q939D2), Burkholderia pseudomallei
Ivancich, A.; Donald, L.J.; Villanueva, J.; Wiseman, B.; Fita, I.; Loewen, P.C.
Spectroscopic and kinetic investigation of the reactions of peroxyacetic acid with Burkholderia pseudomallei catalase-peroxidase, KatG
Biochemistry
52
7271-7282
2013
Burkholderia pseudomallei
Zamocky, M.; Gasselhuber, B.; Furtmueller, P.G.; Obinger, C.
Turning points in the evolution of peroxidase-catalase superfamily molecular phylogeny of hybrid heme peroxidases
Cell. Mol. Life Sci.
71
4681-4696
2014
Burkholderia pseudomallei
Vidossich, P.; Loewen, P.C.; Carpena, X.; Fiorin, G.; Fita, I.; Rovira, C.
Binding of the antitubercular pro-drug isoniazid in the heme access channel of catalase-peroxidase (KatG). A combined structural and metadynamics investigation
J. Phys. Chem. B
118
2924-2931
2014
Burkholderia pseudomallei (Q3JNW6), Burkholderia pseudomallei 1710b (Q3JNW6)
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