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Literature summary for 1.11.1.21 extracted from

  • Ro, Y.T.; Lee, H.I.; Kim, E.J.; Koo, J.H.; Kim, E.; Kim, Y.M.
    Purification, characterization, and physiological response of a catalase-peroxidase in Mycobacterium sp. strain JC1 DSM 3803 grown on methanol (2003), FEMS Microbiol. Lett., 226, 397-403.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
3-Amino-1,2,4-triazole 156% relative catalase activity at 10 mM, 121% relative peroxidase activity at 10 mM Mycobacterium sp.

General Stability

General Stability Organism
the enzyme retains both catalase and peroxidase activities after having been subjected to PAGE in the presence of 0.1% (w/v) SDS, over 90% of the initial catalase and peroxidase activities are detected from enzyme preparations incubated for 5 min in an ethanol-chloroform mixture Mycobacterium sp.

Inhibitors

Inhibitors Comment Organism Structure
hydroxylamine complete inhibition of catalase activity at 1 mM, 42% residual peroxidase activity at 1 mM Mycobacterium sp.
isoniazid
-
Mycobacterium sp.
KCN 4% residual catalase activity at 1 mM, 4% residual peroxidase activity at 1 mM Mycobacterium sp.
additional information the enzyme is resistant to inhibition by 3-amino-1,2,4-triazole Mycobacterium sp.
NaN3 8% residual catalase activity at 1 mM, 1% residual peroxidase activity at 1 mM Mycobacterium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0478
-
o-Dianisidine peroxidase activity, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C Mycobacterium sp.
1.47
-
H2O2 peroxidase activity, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C Mycobacterium sp.
6.3
-
H2O2 catalase activity, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C Mycobacterium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
2 * 80000, SDS-PAGE Mycobacterium sp.
160000
-
gel filtration Mycobacterium sp.

Organism

Organism UniProt Comment Textmining
Mycobacterium sp.
-
formerly Acinetobacter sp.
-
Mycobacterium sp. JC1 DSM 3803
-
formerly Acinetobacter sp.
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, Sepharose 6B column chromatography, DEAE-Sephacel column chromatography, Sephadex G-25 gel filtration, and hydroxylapatite column chromatography Mycobacterium sp.

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:methanol-grown cell
-
Mycobacterium sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
24.2
-
crude extract, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C Mycobacterium sp.
1145
-
after 47.3fold purification, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C Mycobacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2
-
Mycobacterium sp. O2 + H2O
-
?
H2O2
-
Mycobacterium sp. DSM 3803 / JC1 O2 + H2O
-
?
H2O2
-
Mycobacterium sp. JC1 DSM 3803 O2 + H2O
-
?
methanol + H2O2 at pH 4.5 Mycobacterium sp. formaldehyde + H2O
-
?
NADH + H2O2
-
Mycobacterium sp. ?
-
?
o-dianisidine + H2O2
-
Mycobacterium sp. oxidized o-dianisidine + H2O
-
?
o-dianisidine + H2O2
-
Mycobacterium sp. DSM 3803 / JC1 oxidized o-dianisidine + H2O
-
?
o-dianisidine + H2O2
-
Mycobacterium sp. JC1 DSM 3803 oxidized o-dianisidine + H2O
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 80000, SDS-PAGE Mycobacterium sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
peroxidase activity Mycobacterium sp.
40
-
catalase activity Mycobacterium sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
when the purified enzyme is incubated for 1 min at 60°C, catalase and peroxidase activities decrease by over 80% Mycobacterium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
peroxidase activity Mycobacterium sp.
7
-
catalase activity Mycobacterium sp.

Cofactor

Cofactor Comment Organism Structure
heme
-
Mycobacterium sp.

pI Value

Organism Comment pI Value Maximum pI Value
Mycobacterium sp. isoelectric focusing
-
4.8

Expression

Organism Comment Expression
Mycobacterium sp. the peroxidase activity of catalase-peroxidase in cells growing at the late-exponential growth phase (24 h after inoculation) decreases to 25% less than that in cells growing in the absence of isoniazid down
Mycobacterium sp. isoniazid had almost no effect on the expression of catalase-peroxidase additional information
Mycobacterium sp. the peroxidase activity of catalase-peroxidase in sodium nitroprusside-treated cells is 2.7fold higher than that in cells not treated with 1 mM sodium nitroprusside up