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Literature summary for 1.11.1.21 extracted from

  • Moore, R.L.; Cook, C.O.; Williams, R.; Goodwin, D.C.
    Substitution of strictly conserved Y111 in catalase-peroxidases: Impact of remote interdomain contacts on active site structure and catalytic performance (2008), J. Inorg. Biochem., 102, 1819-1824.
    View publication on PubMed
Search for more literature for 1.11.1.21

Protein Variants

Protein Variants Comment Organism
Y111A the mutation leads to a 5fold reduction in the apparent kcat for catalase activity and an 8fold decrease in the apparent second-order rate constant. For peroxidase activity, the H2O2- and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)-dependent peroxidatic apparent kcat are reduced by 66% and 40%, respectively. Preparations of this variant yield a mixture of high- and low-spin heme states, thus creating the appearance of a transition between wild type (high-spin) and C-terminal lacking (low-spin) KatG Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
cyanide
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.061
-
 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
0.07
-
 H2O2 mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
0.087
-
 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
0.18
-
 H2O2 wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
3.5
-
 H2O2 wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C Escherichia coli
5.2
-
 H2O2 mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
-
 Escherichia coli oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
 ?
H2O2
-
 Escherichia coli O2 + H2O
-
 ?

Synonyms

Synonyms Comment Organism
KatG
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
22.4
-
 H2O2 mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
33.3
-
 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
55.2
-
 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
65
-
 H2O2 wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
2140
-
 H2O2 mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C Escherichia coli
11000
-
 H2O2 wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme
-
 Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
320
-
 H2O2 mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
360
-
 H2O2 wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
410
-
 H2O2 mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C Escherichia coli
546
-
 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
634
-
 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C Escherichia coli
3200
-
 H2O2 wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C Escherichia coli