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Literature summary for 1.11.1.21 extracted from

  • Obinger, C.; Regelsberger, G.; Strasser, G.; Burner, U.; Peschek, G.A.
    Purification and characterization of a homodimeric catalase-peroxidase from the cyanobacterium Anacystis nidulans (1997), Biochem. Biophys. Res. Commun., 235, 545-552.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
cyanide
-
Synechococcus elongatus PCC 7942 = FACHB-805
H2O2 purified enzyme is sensitive to H2O2 concentrations higher than 10 mM Synechococcus elongatus PCC 7942 = FACHB-805
additional information the enzyme is insensitive to the eukaryotic catalase inhibitor 3-amino-1,2,4-triazole Synechococcus elongatus PCC 7942 = FACHB-805

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3
-
H2O2 catalase activity, in 67 mM phosphate buffer (pH 7.0), at 25°C Synechococcus elongatus PCC 7942 = FACHB-805

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Synechococcus elongatus PCC 7942 = FACHB-805 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80500
-
2 * 80500, native PAGE Synechococcus elongatus PCC 7942 = FACHB-805

Organism

Organism UniProt Comment Textmining
Synechococcus elongatus PCC 7942 = FACHB-805
-
formerly Synechococcus sp. strain PCC 6301
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, Fractogel EMD 650(s) DEAE column chromatography, phenyl-Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S300 gel filtration Synechococcus elongatus PCC 7942 = FACHB-805

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.4
-
crude extract, in 67 mM phosphate buffer (pH 7.0), at 25°C Synechococcus elongatus PCC 7942 = FACHB-805
785
-
after 178fold purification, in 67 mM phosphate buffer (pH 7.0), at 25°C Synechococcus elongatus PCC 7942 = FACHB-805

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2
-
Synechococcus elongatus PCC 7942 = FACHB-805 O2 + H2O
-
?
additional information the enzyme does not accept electrons from ascorbate, glutathione, and NADH Synechococcus elongatus PCC 7942 = FACHB-805 ?
-
?
o-dianisidine + H2O2
-
Synechococcus elongatus PCC 7942 = FACHB-805 oxidized o-dianisidine + H2O
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 80500, native PAGE Synechococcus elongatus PCC 7942 = FACHB-805

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7200
-
H2O2 catalase activity, in 67 mM phosphate buffer (pH 7.0), at 25°C Synechococcus elongatus PCC 7942 = FACHB-805

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 9 75-80% of maximum initial rates are still retained at pH 6.0 and 9.0 Synechococcus elongatus PCC 7942 = FACHB-805
6.5 7.5 catalase and peroxidase activities Synechococcus elongatus PCC 7942 = FACHB-805

Cofactor

Cofactor Comment Organism Structure
heme
-
Synechococcus elongatus PCC 7942 = FACHB-805

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0272
-
cyanide in 67 mM phosphate buffer (pH 7.0), at 25°C Synechococcus elongatus PCC 7942 = FACHB-805

pI Value

Organism Comment pI Value Maximum pI Value
Synechococcus elongatus PCC 7942 = FACHB-805 isoelectric focusing
-
4.7