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Literature summary for 1.11.1.21 extracted from

  • Jakopitsch, C.; Rueker, F.; Regelsberger, G.; Dockal, M.; Peschek, G.A.; Obinger, C.
    Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803: cloning, overexpression in Escherichia coli, and kinetic characterization (1999), Biol. Chem., 380, 1087-1096.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) pLysS cells Synechocystis sp.

Inhibitors

Inhibitors Comment Organism Structure
azide
-
Synechocystis sp.
cyanide
-
Synechocystis sp.
additional information the enzyme is not inhibited by 3-amino-1,2,4-triazole Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.9
-
H2O2 catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C Synechocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
85000
-
2 * 85000, SDS-PAGE Synechocystis sp.
85122
-
2 * 85122, MALDI-TOF mass spectrometry Synechocystis sp.
85137
-
2 * 85137, calculated from amino acid sequence Synechocystis sp.
170000
-
gel filtration Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Zn2+-chelate affinity chromatography and phenyl-Sepharose column chromatography Synechocystis sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.61
-
crude enzyme, peroxidase activity, in 67 mM phosphate buffer, pH 7.0, at 25°C Synechocystis sp.
1.7
-
after 2.79fold purification, peroxidase activity, in 67 mM phosphate buffer, pH 7.0, at 25°C Synechocystis sp.
368
-
crude enzyme, catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C Synechocystis sp.
983
-
after 2.67fold purification, catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
-
Synechocystis sp. oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
?
guaiacol + H2O2
-
Synechocystis sp. tetraguaiacol + H2O
-
?
H2O2
-
Synechocystis sp. O2 + H2O
-
?
additional information the recombinant protein contains high catalase activity and an appreciable peroxidase activity with o-dianisidine, guaiacol and pyrogallol, but not with NAD(P)H, ferrocytochrome c, ascorbate or glutathione as electron donors Synechocystis sp. ?
-
?
o-dianisidine + H2O2
-
Synechocystis sp. oxidized o-dianisidine + H2O
-
?
pyrogallol + H2O2
-
Synechocystis sp. ? + H2O
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 85000, SDS-PAGE Synechocystis sp.
homodimer 2 * 85122, MALDI-TOF mass spectrometry Synechocystis sp.
homodimer 2 * 85137, calculated from amino acid sequence Synechocystis sp.

Synonyms

Synonyms Comment Organism
EC 1.11.1.7 formerly Synechocystis sp.
KatG
-
Synechocystis sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3500
-
H2O2 catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
heme
-
Synechocystis sp.

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.037
-
cyanide in 67 mM phosphate buffer, pH 7.0, at 30°C Synechocystis sp.
0.051
-
azide in 67 mM phosphate buffer, pH 7.0, at 30°C Synechocystis sp.

pI Value

Organism Comment pI Value Maximum pI Value
Synechocystis sp. isoelectric focusing
-
5.4

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
710
-
H2O2 catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C Synechocystis sp.