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Information on EC 1.11.1.21 - catalase-peroxidase and Organism(s) Haloarcula marismortui and UniProt Accession O59651

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.21 catalase-peroxidase
IUBMB 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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Haloarcula marismortui
UNIPROT: O59651
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The taxonomic range for the selected organisms is: Haloarcula marismortui
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hide
donor
+
H2O2
=
oxidized donor
+
2
H2O
+
=
+
2
2
H2O2
=
O2
+
2
H2O
2
=
+
2
Synonyms
catalase-peroxidase, catalase peroxidase, catalase/peroxidase, hydroperoxidase i, katg2, katx2, katg1, fvcp02, fvcp01, afkatg, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
catalase-peroxidase
-
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
show the reaction diagram
-
-
-
-
?
diaminobenzidine + H2O2
oxidized diaminobenzidine + H2O
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
isoniazid + H2O2
?
show the reaction diagram
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
show the reaction diagram
-
-
-
-
?
pyrogallol + H2O2
? + H2O
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
-
the peroxidatic activity on diaminobenzidine shows a continuous decrease with increasing NaCl concentration
additional information
-
no inhibition of the catalase activity of hCP is seen with 3-amino-l,2,4-triazole
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ammonium sulfate
-
additions of ammonium sulfate even at weak concentrations (10 to 70 mM) stimulate catalatic activity measured in the presence of 1.5 M NaC1 by about 30%
NaCl
-
with NaC1, maximum activity is observed near 0.5-0.7 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 2.5
H2O2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
crude extract, catalatic activity, at 20°C and pH 7.5, in the presence of 1.5 M NaC1
851
-
after 170fold purification, catalatic activity, at 20°C and pH 7.5, in the presence of 1.5 M NaC1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
peroxidatic activity in the absence of NaCl, with diaminobenzidine as electron donor
7.5
-
catalatic activity in molar concentrations of NaCl, with diaminobenzidine as electron donor
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
81254
x * 81254, calculated from sequence
81292
x * 81292, mass spectrometry
81290
-
mass spectrometry
94000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
each subunit is composed of two structurally homologous domains with a topology similar to that of class I peroxidase
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, the rhombic plate-shaped crystals are grown from purified protein solution using (NH4)2SO4 as precipitant at 20°C. The crystal belongs to the monoclinic system, space group C2, and diffract beyond 2.0 A resolution
the 2.0 A crystal structure of the enzyme reveals that it is a dimer of two identical subunits. Each subunit is composed of two structurally homologous domains with a topology similar to that of class I peroxidase. The active site is in the N-terminal domain. Although the arrangement of the catalytic residues and the cofactor heme b in the active site is virtually identical to that of class I peroxidases, the heme moiety is buried inside the domain, similar to that in a typical catalase. In the vicinity of the active site, novel covalent bonds are formed among the side chains of three residues, including that of a tryptophan on the distal side of the heme. Together with the C-terminal domain, these covalent bonds fix two long loops on the surface of the enzyme that cover the substrate access channel to the active site. These features provide an explanation for the dual activities of this enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Sepharose column chromatography, DEAE cellulose column chromatography, dialysis, hydroxyapatite column chromatography, and ACA 44 gel filtration
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
Cendrin, F.; Jouve, H.M.; Gaillard, J.; Thibault, P.; Zaccai, G.
Purification and properties of a halophilic catalase-peroxidase from Haloarcula marismortui
Biochim. Biophys. Acta
1209
1-9
1994
Haloarcula marismortui
Manually annotated by BRENDA team
Yamada, Y.; Saijo, S.; Sato, T.; Igarashi, N.; Usui, H.; Fujiwara, T.; Tanaka, N.
Crystallization and preliminary X-ray analysis of catalase-peroxidase from the halophilic archaeon Haloarcula marismortui
Acta Crystallogr. Sect. D
57
1157-1158
2001
Haloarcula marismortui (O59651), Haloarcula marismortui, Haloarcula marismortui DSM 3752 (O59651)
Manually annotated by BRENDA team
Cannac-Caffrey, V.; Hudry-Clergeon, G.; Petillot, Y.; Gagnon, J.; Zaccai, G.; Franzetti, B.
The protein sequence of an archaeal catalase-peroxidase
Biochimie
80
1003-1011
1998
Haloarcula marismortui (O59651), Haloarcula marismortui, Haloarcula marismortui DSM 3752 (O59651)
Manually annotated by BRENDA team
Yamada, Y.; Fujiwara, T.; Sato, T.; Igarashi, N.; Tanaka, N.
The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui
Nat. Struct. Biol.
9
691-695
2002
Haloarcula marismortui (O59651), Haloarcula marismortui, Haloarcula marismortui DSM 3752 (O59651)
Manually annotated by BRENDA team
Fita, I.; Carpena, X.; Loewen, P.
Chapter 7 Catalase-peroxidase (KatG) structure and function
RSC Metallobiol.
2016
135-155
2016
Haloarcula marismortui
-
Manually annotated by BRENDA team