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1.11.1.6: catalase

This is an abbreviated version!
For detailed information about catalase, go to the full flat file.

Word Map on EC 1.11.1.6

Reaction

2 H2O2 =

O2
+ 2 H2O

Synonyms

Ab-catalase, BNC, caperase, CAT, CAT-1, CAT-A, CAT-P, Cat1.4, CatA, catalase, catalase A, catalase C, catalase form III, catalase P, catalase-1, catalase-A, catalase-peroxidase, catalase-phenol oxidase, CatB, CATC, CatF, CatG, CatP, CATPO, CcmC, CP, equilase, H2O2:H2O2 oxidoreductase, haem catalase, HPI-A, HPI-B, HPII, HTHP, hydrogen peroxide oxidoreductase, KAT, Kat E catalase, KatA, KatB, KatC, KatP, KpA, manganese catalase, More, optidase, PktA, polyethylene glycol-catalase, tyrosine-coordinated heme protein, VktA

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.6 catalase

Engineering

Engineering on EC 1.11.1.6 - catalase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S2W
-
natural polymorphism. Strain S carries the Ser isoform, strain G3 carries the Trp-isoform which shows a lower specific activity and higher Km value than the Ser-isoform. Mutation S2W destabilizes the functional tetrameric form of the enzyme. Ser/Ser females have a significantly higher fecundity than Trp/Trp females
D270A
-
site-directed mutagenesis
H146A
-
site-directed mutagenesis
H215A
-
site-directed mutagenesis
H55A
-
site-directed mutagenesis
N376A
-
site-directed mutagenesis
N82A
-
site-directed mutagenesis
P391A
-
site-directed mutagenesis
Q332A
-
site-directed mutagenesis
R6A
-
site-directed mutagenesis
V210A
-
site-directed mutagenesis
W257A
-
site-directed mutagenesis
Y117A
-
site-directed mutagenesis
Y338A
-
site-directed mutagenesis
Y397A
-
site-directed mutagenesis
D474N
-
site-directed mutagenesis, catalase inactive mutant
H473N
-
site-directed mutagenesis, catalase inactive mutant
Y111A
-
substantial increase in hexa-xoordinate low-spin heme with the appearance of a transition between the wild-type primarily high-spin and the N-terminal pure low-spin domain alone. Decrease in activity is for catalase activity more substantially than for peroxidase activity
M244A
-
coplete loss of catalase activity, increased peroxidase activity due to enhanced affinity for the peroidatic substrate
S315T
-
mutation at katG codon 315 detected in 17 (63.0%) of the 27 isoniazid-resistant isolates analyzed. The most prevalent mutation observed is AGC315ACC (Ser315Thr), involving 11(65%) of the 17 isoniazid-resistant isolates having a mutation in the sequenced region. Ten isoniazid-resistant and all 29 isoniazid-susceptible isolates sequenced have no mutation in this region. Of the 19 multi-drug-resistant isolates, 15 (78.9%) show a mutation in codon 315, while only two (25%) of the eight isoniazid mono-resistant isolates are found to have a mutation in that codon
W107F
-
mutation in key distal side residue, disrupts high-affinity binding of substrate isonicotinic hydrazide
Y229F
-
mutation in key distal side residue, disrupts high-affinity binding of substrate isonicotinic hydrazide
E316F
kcat/Km is 2fold lower than kcat/Km for wild-type enzyme
E316H
kcat/Km is 2.6fold lower than kcat/Km for wild-type enzyme
H246W
kcat/Km is 5.3fold lower than kcat/Km for wild-type enzyme
H82N
-
site-directed mutagenesis, the mutation results in conversion of the native d-type heme to a b-type heme
I313F
slight increase in kcat/Km as compared to kcat/Km of wild-type enzyme
I314F
kcat/Km is 5.2fold lower than kcat/Km for wild-type enzyme
L321A
kcat/Km is 1.2fold lower than kcat/Km for wild-type enzyme
V123F
-
site-directed mutagenesis
V536A
kcat/Km is 1.6fold lower than kcat/Km for wild-type enzyme
V536W
kcat/Km is 5.1fold lower than kcat/Km for wild-type enzyme
H82N
-
site-directed mutagenesis, the mutation results in conversion of the native d-type heme to a b-type heme
-
V123F
-
site-directed mutagenesis
-
L189W/H225T
almost 3fold decrease in Km-value, 2-2.5fold increase in enzyme velocity, loss of photoinhibition
M129V/E293G
less thermostable mutant enzyme
H72A
KTL38510
mutant in heme-binding residue, almost complete loss of activity
V71A and F158A
KTL38510
channel point mutant, about 20% of wild-type activity
Y353A
KTL38510
mutant in heme-binding residue, almost complete loss of activity
H72A
-
mutant in heme-binding residue, almost complete loss of activity
-
V71A and F158A
-
channel point mutant, about 20% of wild-type activity
-
Y353A
-
mutant in heme-binding residue, almost complete loss of activity
-
additional information