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Literature summary for 1.11.1.21 extracted from

  • Smulevich, G.; Jakopitsch, C.; Droghetti, E.; Obinger, C.
    Probing the structure and bifunctionality of catalase-peroxidase (KatG) (2006), J. Inorg. Biochem., 100, 568-585.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Synechococcus sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Burkholderia pseudomallei
-
Mycobacterium tuberculosis
-
Synechococcus sp.

Protein Variants

Protein Variants Comment Organism
D141A the mutant shows 1.5% of wild type catalase activity and 132% of wild type peroxidase activity Burkholderia pseudomallei
D141E the mutant shows 80% of wild type catalase activity and 143% of wild type peroxidase activity Burkholderia pseudomallei
D141N the mutant shows 10% of wild type catalase activity and 123% of wild type peroxidase activity Burkholderia pseudomallei
D152N the mutant shows 2.7% of wild type catalase activity and 234% of wild type peroxidase activity Synechococcus sp.
D152S the mutant shows 5.7% of wild type catalase activity and 237% of wild type peroxidase activity Synechococcus sp.
D152W the mutant shows 0.6% of wild type catalase activity and 672% of wild type peroxidase activity Synechococcus sp.
D402E the mutant shows 0.6% of wild type catalase activity and 65% of wild type peroxidase activity Synechococcus sp.
D402N the mutant shows 0.5% of wild type catalase activity and 56% of wild type peroxidase activity Synechococcus sp.
E253D the mutant shows 42% of wild type catalase activity and 280% of wild type peroxidase activity Synechococcus sp.
E253Q the mutant shows 25% of wild type catalase activity and 96% of wild type peroxidase activity Synechococcus sp.
H106C the mutant shows 0.01% of wild type catalase activity and 1.7% of wild type peroxidase activity Escherichia coli
H106Y the mutant shows 0.008% of wild type catalase activity and 2.7% of wild type peroxidase activity Escherichia coli
H108Q the mutant shows 0.03% of wild type catalase activity and 47% of wild type peroxidase activity Mycobacterium tuberculosis
H112A the mutant shows 0.02% of wild type catalase activity and 2.3% of wild type peroxidase activity Burkholderia pseudomallei
H112N the mutant shows 0.05% of wild type catalase activity and 2.3% of wild type peroxidase activity Burkholderia pseudomallei
H123E the mutant shows 0.03% of wild type catalase activity and 13% of wild type peroxidase activity Synechococcus sp.
H123Q the mutant shows 0.02% of wild type catalase activity and 7.4% of wild type peroxidase activity Synechococcus sp.
H257Y the mutant shows 0.05% of wild type catalase activity and 1.8% of wild type peroxidase activity Escherichia coli
H290Q the mutant shows 0.09% of wild type catalase activity and 5.6% of wild type peroxidase activity Synechococcus sp.
I248F the mutant shows 12% of wild type catalase activity and 124% of wild type peroxidase activity Synechococcus sp.
M264A the mutant shows 0.15% of wild type catalase activity and 160% of wild type peroxidase activity Burkholderia pseudomallei
M264L the mutant shows 0.02% of wild type catalase activity and 140% of wild type peroxidase activity Burkholderia pseudomallei
M275I the mutant shows 0.6% of wild type catalase activity and 640% of wild type peroxidase activity Synechococcus sp.
N153A the mutant shows 6% of wild type catalase activity and 60% of wild type peroxidase activity Synechococcus sp.
N153D the mutant shows 17% of wild type catalase activity and 130% of wild type peroxidase activity Synechococcus sp.
N251L the mutant shows 33% of wild type catalase activity and 415% of wild type peroxidase activity Synechococcus sp.
P252A the mutant shows 110% of wild type catalase activity and 97% of wild type peroxidase activity Synechococcus sp.
R102C the mutant shows 0.5% of wild type catalase activity and 10% of wild type peroxidase activity Escherichia coli
R102K the mutant shows 1.8% of wild type catalase activity and 13% of wild type peroxidase activity Escherichia coli
R102L the mutant shows 1% of wild type catalase activity and 13% of wild type peroxidase activity Escherichia coli
R104L the mutant shows 0.06% of wild type catalase activity and 200% of wild type peroxidase activity Mycobacterium tuberculosis
R108A the mutant shows 31% of wild type catalase activity and 23% of wild type peroxidase activity Burkholderia pseudomallei
R108K the mutant shows 8% of wild type catalase activity and 21% of wild type peroxidase activity Burkholderia pseudomallei
R119A the mutant shows 15% of wild type catalase activity and 12% of wild type peroxidase activity Synechococcus sp.
R119N the mutant shows 0.5% of wild type catalase activity and 5% of wild type peroxidase activity Synechococcus sp.
R418L the mutant shows 0.6% of wild type catalase activity and 192% of wild type peroxidase activity Mycobacterium tuberculosis
R426A the mutant shows 4.3% of wild type catalase activity and 99% of wild type peroxidase activity Burkholderia pseudomallei
R426K the mutant shows 70% of wild type catalase activity and 97% of wild type peroxidase activity Burkholderia pseudomallei
R439A the mutant shows 4.9% of wild type catalase activity and 12% of wild type peroxidase activity Synechococcus sp.
R439N the mutant shows 3.1% of wild type catalase activity and 100% wild type peroxidase activity Synechococcus sp.
S315T the mutant shows 52% of wild type catalase activity and 50% of wild type peroxidase activity Mycobacterium tuberculosis
S324T the mutant shows 109% of wild type catalase activity and 94% of wild type peroxidase activity Burkholderia pseudomallei
S335T the mutant shows 99% of wild type catalase activity and 103% of wild type peroxidase activity Synechococcus sp.
W105F the mutant shows 0.1% of wild type catalase activity and 288% of wild type peroxidase activity Escherichia coli
W105L the mutant shows 0.3% of wild type catalase activity and 197% of wild type peroxidase activity Escherichia coli
W111F the mutant shows 0.05% of wild type catalase activity and 75% of wild type peroxidase activity Burkholderia pseudomallei
W122A the mutant shows no catalase activity and 100% wild type peroxidase activity Synechococcus sp.
W122F the mutant shows no catalase activity and 90% of wild type peroxidase activity Synechococcus sp.
W321F the mutant shows 38% of wild type catalase activity and 18% of wild type peroxidase activity Mycobacterium tuberculosis
W341A the mutant shows 0.5% of wild type catalase activity and 25% of wild type peroxidase activity Synechococcus sp.
W341F the mutant shows 42% of wild type catalase activity and 190% of wild type peroxidase activity Synechococcus sp.
Y229F the mutant shows 0.002% of wild type catalase activity and 1360% of wild type peroxidase activity Mycobacterium tuberculosis
Y238A the mutant shows 0.05% of wild type catalase activity and 140% of wild type peroxidase activity Burkholderia pseudomallei
Y238F the mutant shows 0.15% of wild type catalase activity and 64% of wild type peroxidase activity Burkholderia pseudomallei
Y249F the mutant shows 0.17% of wild type catalase activity and 121% of wild type peroxidase activity Synechococcus sp.

Organism

Organism UniProt Comment Textmining
Burkholderia pseudomallei Q939D2
-
-
Escherichia coli
-
-
-
Mycobacterium tuberculosis P9WIE5
-
-
Mycobacterium tuberculosis H37Rv P9WIE5
-
-
Synechococcus sp. Q31MN3
-
-
Synechococcus sp. PCC 7942 Q31MN3
-
-

Synonyms

Synonyms Comment Organism
KatG
-
Escherichia coli
KatG
-
Burkholderia pseudomallei
KatG
-
Mycobacterium tuberculosis
KatG
-
Synechococcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
peroxidase activity of KatG Escherichia coli
5.5
-
peroxidase activity of KatG Burkholderia pseudomallei
5.5
-
peroxidase activity of KatG Mycobacterium tuberculosis
5.5
-
peroxidase activity of KatG Synechococcus sp.

Cofactor

Cofactor Comment Organism Structure
heme
-
Escherichia coli
heme
-
Burkholderia pseudomallei
heme
-
Mycobacterium tuberculosis
heme ferric and ferrous KatG show predominant five-coordinate high-spin heme. However, the ferric form shows also small amounts of both six-coordinate high-spin and six-coordinate low-spin, and the ferrous form also exhibits a 6-coordinate low-spin heme Synechococcus sp.