1.11.1.13: manganese peroxidase

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

Word Map on EC 1.11.1.13

Reaction

2 Mn(II) + 2 H+ +

H2O2
= 2 Mn(III) + 2 H2O

Synonyms

hybrid Mn-peroxidase, L-MnP, LeMnP2, manganese peroxidase, manganese-dependent peroxidase, Mn-dependent (NADH-oxidizing) peroxidase, Mn2+: hydrogen peroxide oxidoreductase, Mn2+:hydrogen peroxide oxidoreductase, MnP, MnP 1, MnP II, MnP-GY, MnP-PGY, mnp1, MnP2, MnP3, MnP6, MP, multifunctional manganese peroxidase, Nf b19 MNP2, peroxidase, manganese, peroxidase-M2

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.13 manganese peroxidase

Engineering

Engineering on EC 1.11.1.13 - manganese peroxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S168W
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
S168W
-
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
-
T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G
-
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
-
A48C/A63C
-
A48C and A63C double mutant with an engineered disulfide bond near the distal calcium binding site to restrict the movement of helix B upon loss of calcium and to stabilize against this loss, thermal and pH-stability is improved compared with that of native and recombinant MnP, thermally treated enzyme contains one calcium and retains a percentage of its activity
E35Q
-
engineered mutant
F190A
-
mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
F190I
-
mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
F190L
-
rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
F190Y
-
engineered mutant
M237L
engineered mutant
M273L
mutant with high H2O2 resistance, i.e. 4.1fold higher than that of wild-type, Met-273 is located near the active site pocket and is converted to a non-oxidizable Leu
M67L
engineered mutant
N131D
-
mutant displays a similar catalysis pattern to that of wild-type enzyme, Asn131 is the only potential glycosylation site
N81S
mutant enzyme is not inhibited by 1 mM H2O2, H2O2-dependency is 5.5fold higher than that of wild-type, engineering of Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
R177A
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177D
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177E
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177K
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177N
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177Q
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R42A
-
mutant displays a similar catalysis pattern to that of wild-type enzyme, Arg42 is forming the peroxide binding pocket
S168W
-
mutant can oxidize both Mn2+ and typical lignin peroxidase substrates such as veratryl alcohol
F190A
-
mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
-
F190I
-
mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
-
F190L
-
rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
-
F190Y
-
engineered mutant
-
R177A
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
-
R177D
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
R177E
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
R177K
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
-
R177N
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-