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Literature summary for 1.11.1.21 extracted from

  • Marcinkeviciene, J.A.; Magliozzo, R.S.; Blanchard, J.S.
    Purification and characterization of the Mycobacterium smegmatis catalase-peroxidase involved in isoniazid activation (1995), J. Biol. Chem., 270, 22290-22295.
    View publication on PubMed
Search for more literature for 1.11.1.21

Inhibitors

Inhibitors Comment Organism Structure
isoniazid i.e. isonicotinic acid hydrazide, strong competitive inhibition Mycolicibacterium smegmatis
Isonicotinic acid hydrazide
-
 Mycolicibacterium smegmatis
KCN competitive inhibition against tert-butyl hydroperoxide Mycolicibacterium smegmatis
additional information not inhibited by 3-amino-1,2,4-triazole, nicotinamide, isonicotinamide or pyrazinamide Mycolicibacterium smegmatis
NaN3 weak competitive inhibition against o-dianisidine Mycolicibacterium smegmatis
nicotinic acid hydrazide strong competitive inhibition Mycolicibacterium smegmatis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.11
-
 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) peroxidatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis
0.14
-
 o-Dianisidine peroxidatic activity, with hydrogen peroxide as cosubstrate, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis
0.14
-
 o-Dianisidine peroxidatic activity, with tert-butyl hydroperoxide as cosubstrate, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis
0.17
-
 NADPH peroxidatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis
0.23
-
 NADH peroxidatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis
0.31
-
 pyrogallol peroxidatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis
0.6
-
 H2O2 catalatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
 4 * 80000, SDS-PAGE Mycolicibacterium smegmatis
81889
-
 4 * 81889, calculated from amino acid sequence Mycolicibacterium smegmatis
330000
-
 gel filtration Mycolicibacterium smegmatis

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis
-
-
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose column chromatography, Superdex 200 gel filtration, Mono Q column chromatography, and phenyl-Superose column chromatography Mycolicibacterium smegmatis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5
-
 crude extract, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis
533
-
 after 214fold purification, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
-
 Mycolicibacterium smegmatis oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
 ?
3,3'-diaminobenzidine + H2O2
-
 Mycolicibacterium smegmatis oxidized 3,3'-diaminobenzidine + H2O
-
 ?
H2O2
-
 Mycolicibacterium smegmatis O2 + H2O
-
 ?
H2O2
-
 Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 O2 + H2O
-
 ?
additional information the enzyme is very slowly reduced by dithionite Mycolicibacterium smegmatis ?
-
 ?
additional information the enzyme is very slowly reduced by dithionite Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 ?
-
 ?
NADH + H2O2
-
 Mycolicibacterium smegmatis ?
-
 ?
NADH + H2O2
-
 Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 ?
-
 ?
NADPH + H2O2
-
 Mycolicibacterium smegmatis ?
-
 ?
o-dianisidine + H2O2
-
 Mycolicibacterium smegmatis oxidized o-dianisidine + H2O
-
 ?
o-dianisidine + H2O2
-
 Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 oxidized o-dianisidine + H2O
-
 ?
o-dianisidine + tert-butyl hydroperoxide
-
 Mycolicibacterium smegmatis oxidized o-dianisidine + ?
-
 ?
pyrogallol + H2O2
-
 Mycolicibacterium smegmatis ? + H2O
-
 ?
pyrogallol + H2O2
-
 Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 ? + H2O
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 80000, SDS-PAGE Mycolicibacterium smegmatis
homotetramer 4 * 81889, calculated from amino acid sequence Mycolicibacterium smegmatis

Cofactor

Cofactor Comment Organism Structure
heme catalase-peroxidase contains 2 heme molecules per tetramer Mycolicibacterium smegmatis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.003
-
 KCN using tert-butyl hydroperoxide as substrate, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis
0.0043
-
 Isonicotinic acid hydrazide using o-dianisidine as substrate, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis
0.0053
-
 nicotinic acid hydrazide using o-dianisidine as substrate, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis
1.1
-
 NaN3 using o-dianisidine as substrate, in 50 mM phosphate buffer, pH 7.0, at 25°C Mycolicibacterium smegmatis

General Information

General Information Comment Organism
physiological function catalase-peroxidase is involved in isoniazid activation Mycolicibacterium smegmatis