Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.11.1.28: lipoyl-dependent peroxiredoxin

This is an abbreviated version!
For detailed information about lipoyl-dependent peroxiredoxin, go to the full flat file.

Word Map on EC 1.11.1.28

Reaction

a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine
+
ROOH
=
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine
 +
H2O
 +
ROH

Synonyms

AhpC, AhpCD, AhpD, ahpD1, ahpD2, alkyl hydroperoxide reductase, alkyl hydroperoxide reductase subunit C, EC 1.11.1.15, MfOhr, Ohr, Organic hydroperoxide resistance, organic hydroperoxide resistance protein, peroxiredoxin AhpC, peroxiredoxin AhpD

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.28 lipoyl-dependent peroxiredoxin

Engineering

Engineering on EC 1.11.1.28 - lipoyl-dependent peroxiredoxin

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C130S
expressed in yield comparable to that of the wild-type protein. Mutation decreases activity to less than 5% of the wild-type enzyme
C133S
expressed in yield comparable to that of the wild-type protein. Mutation completely suppresses the activity
C174S
mutant enzyme retains about 10% of the wild-type activity
C176S
mutant enzyme retains about 10% of the wild-type activity
C61S
inactive mutant enzyme
Cys129
mutant enzyme shows no activity with cumene hydroperoxide
Cys132
mutant enzyme retains about 5% of the wild-type activity with cumene hydroperoxide
E118F
expressed at 20% of the wild-type expression level. Mutation decreases catalytic activity
E118Q
expressed at 20% of the wild-type expression level. Mutation modestly loweres the catalytic activity
H132F
expressed in yield comparable to that of the wild-type protein. Mutation decreases the catalytic activity
H132Q
mutant tends to unfold and degrade relatively easily. Mutation decreases the catalytic activity. The H137Q mutation decreases the activity more severely than the H132Q mutation
H137F
expressed in yield comparable to that of the wild-type protein. Mutation decreases the catalytic activity
H137Q
expressed at 20% of the wild-type expression level. Mutation decreases the catalytic activity. The H137Q mutation decreases the activity more severely than the H132Q mutation
C130S
-
expressed in yield comparable to that of the wild-type protein. Mutation decreases activity to less than 5% of the wild-type enzyme
-
C133S
-
expressed in yield comparable to that of the wild-type protein. Mutation completely suppresses the activity
-
C174S
-
mutant enzyme retains about 10% of the wild-type activity
-
C176S
-
mutant enzyme retains about 10% of the wild-type activity
-
C61S
-
inactive mutant enzyme
-
Cys129
-
mutant enzyme shows no activity with cumene hydroperoxide
-
Cys132
-
mutant enzyme retains about 5% of the wild-type activity with cumene hydroperoxide
-
E118Q
-
expressed at 20% of the wild-type expression level. Mutation modestly loweres the catalytic activity
-
H132Q
-
mutant tends to unfold and degrade relatively easily. Mutation decreases the catalytic activity. The H137Q mutation decreases the activity more severely than the H132Q mutation
-
H137Q
-
expressed at 20% of the wild-type expression level. Mutation decreases the catalytic activity. The H137Q mutation decreases the activity more severely than the H132Q mutation
-
C154S
mutant enzyme loses peroxidase activity. The enzyme shows no activity and no formation of intramolecular disulfide bond upon treatment with hydroperoxides
C87S
mutant enzyme loses peroxidase activity. The enzyme shows no activity and no formation of intramolecular disulfide bond upon treatment with hydroperoxides
C154S
-
mutant enzyme loses peroxidase activity. The enzyme shows no activity and no formation of intramolecular disulfide bond upon treatment with hydroperoxides
-
C87S
-
mutant enzyme loses peroxidase activity. The enzyme shows no activity and no formation of intramolecular disulfide bond upon treatment with hydroperoxides
-