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

Subunits

Subunits 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.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
-
the redox state of AhpC is a key factor determining the dimer-decamer equilibrium. at 25 °C exists predominantly as a decamer
dimer
-
the redox state of AhpC is a key factor determining the dimer-decamer equilibrium. at 25 °C exists predominantly as a decamer
oligomer
-
heat induces oligomerization of AhpC. At 53°C the oxidized AhpC forms an high-molecular-weight oligomer with a molecular mass of about 2.0-3.0 MDa, corresponding to 100-150 subunits