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1.11.1.7: peroxidase

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

Word Map on EC 1.11.1.7

Reaction

2 phenolic donor +

H2O2
= 2 phenoxyl radical of the donor + 2 H2O

Synonyms

acidic peroxidase, acidic POD, ALSP, AnaPX, anionic isoperoxidase, anionic peroxidase A1, AOPTP, basic peroxidase, basic POD, BCcP, black radish peroxidase A, black radish peroxidase B, BRP-A, BRP-B, cationic peroxidase, cationic peroxidase Cs, class III plant peroxidase, CmMnP, constitutive peroxidase, CP, cPOD-I, CYP119, dehaloperoxidase A, dehaloperoxidase B, DHP A, donor: H2O2 oxidoreductase, donor: hydrogen peroxide oxidoreductase, donor:hydrogen peroxide oxidoreductase, DtpA, ECPOX, ECPOX 1, ECPOX 2, ECPOX 3, ELP, eosinophil peroxidase, EPO, extensin peroxidase, extracellular peroxidase, FP1, Fp2, FP3, GCP1, GCP2, guaiacol peroxidase, H2O2 oxidoreductase, Hb peroxidase, Hb1, heme peroxidase, hemoglobin 1, hemoglobin peroxidase, hexacoordinate (class 1) non-symbiotic hemoglobin, horseradisch peroxidase, horseradish peroxidase, horseradish peroxidase (HRP), horseradish peroxidase C, HP, HRP, HRP A2, HRP C1A, HRP-C, HRPC, HRPO, HRP_A2A, HRP_C1A, HRP_E5, HTHP, hydrogen donor oxidoreductase, Japanese radish peroxidase, lactoperoxidase, LPO, LPRX, LPS, MAP-2744c, MGP, MnP124076, MnP13, More, MPO, myeloperoxidase, neutral peroxidase, neutral POD, NGO_0994, nsHb-1, oxyperoxidase, p20, PA1, PerII, peroxidase, peroxidase isoenzyme E5, POC1, POD, POD1, POII, POX, POX I, POX II, POX2, protoheme peroxidase, Prx02, Prx03, Prx06, Prx07, Prx09, Prx1, Prx11, Prx114, Prx12, Prx13, Prx15, Prx17, Prx21, Prx22, Prx27, Prx28, Prx30, Prx31, Prx32, Prx33, Prx34, Prx36, Prx37, Prx39, Prx42, Prx43, Prx45, Prx49, Prx50, Prx51, Prx52, Prx53, Prx55, Prx56, Prx57, Prx58, Prx59, Prx60, Prx62, Prx64, Prx66, Prx67, Prx68, Prx69, Prx70, Prx71, Prx72, Prx73, pyrocatechol peroxidase, QPO, quinol peroxidase, rhEPO, rHRP1, rHRP2, royal palm tree peroxidase, rPOD-II, RPTP, rubrerythrin, SacD, Saci_2081, SBP, scavengase, scopoletin peroxidase, SfmD, short PMnP, SPC4, Ssp, stigma-specific peroxidase, thiocyanate peroxidase, thiol peroxidase, TOP, TP I, Tpx, tyrosine-coordinated heme protein, vacuolar class III peroxidase, vascular peroxidase 1, verdoperoxidase, versatile peroxidase, versatile peroxidase VPL2, VP, VPO1, VPO2, WPTP

ECTree

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

Engineering

Engineering on EC 1.11.1.7 - peroxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F130A/F142A/ F143A/F179A
isoform HRP C, mutant shows marginal improvement in stability
F142A
isoform HRP C, mutation in a residue vulnerable to modification by phenoxyl radicals, mutant still exhibits rapid radical inactivation
F143A
isoform HRP C, mutation in a residue vulnerable to modification by phenoxyl radicals, mutant still exhibits rapid radical inactivation
F179A
isoform HRP C, mutation in a residue vulnerable to modification by phenoxyl radicals, mutant still exhibits rapid radical inactivation
F68A
isoform HRP C, mutation in a residue vulnerable to modification by phenoxyl radicals, mutant still exhibits rapid radical inactivation
F68A/F142A/F143A/F179A
isoform HRP C, dramatic enhancement of radical stability by retaining 41% of its initial activity in conditions when wild-type is completely inactivated
N13D/N57S/N255D/N268D
mutations introduced to reduce glycosylation during production in Pichia pastoris
T171S
loss of a structural restraint in the proximal heme pocket that allows slippage of the proximal heme ligand, but only in the reduced state. This is a remarkably subtle and specific effect that appears to increase the flexibility of the reduced state of the mutant compared to that of the wild-type protein. Significant change in the Fe2+/Fe3+ redox potential of the mutant T171S
F41L
Armoracia sp.
-
expressed in Trichoplusia ni cells, full activity
F41T
Armoracia sp.
-
expressed in Trichoplusia ni cells, full activity
C317A
-
the heme content of the mutant is very low and the mutant loses the ability to hydroxylate 3-methyltyrosine
C61S
no activity
C82S
72% of wild-type activity
C82S/C95S
10% of wild-type activity
C95S
20% of wild-type activity
H191A
-
the mutant loses the ability to hydroxylate 3-methyltyrosine
H274A
-
the mutant loses the ability to hydroxylate 3-methyltyrosine
H313A
-
the heme content of the mutant is very low and the mutant loses the ability to hydroxylate 3-methyltyrosine
H232F
P76F
kcat/KM for veratryl alcohol is increased slightly. kcat/KM for Mn2+ as substrate is 2.3fold lower than the wild-type value
W164S
mutant enzyme is completely unable to oxidize both veratryl, alcohol and Reactive Black 5. kcat/KM for Mn2+ as substrate is 1.2fold higher than the wild-type value
W164S/P76H
mutant enzyme is completely unable to oxidize both veratryl, alcohol and Reactive Black 5. kcat/KM for Mn2+ as substrate is 1.1fold lower than the wild-type value
T213A
T213A/T214A
T213F
no formation of styrene epoxide. Protein melting temperature is 2.4°C lower compared to wild-type enzyme
T213S
formation of styrene epoxide is 19% compared to wild-type enzyme. Protein melting temperature is 2°C lower compared to wild-type enzyme
T213V
formation of styrene epoxide is 0.7% compared to wild-type enzyme. Protein melting temperature is 1.1°C lower compared to wild-type enzyme
T213W
T214A
formation of styrene epoxide is 2.7fold higher as compared to wild-type enzyme. Protein melting temperature is 1.6°C lower compared to wild-type enzyme
T214V
formation of styrene epoxide is 2.9fold higher as compared to wild-type enzyme. Protein melting temperature is 2.3°C higher as compared to wild-type enzyme. Mutant is separated into two distinct bands during chromatofocusing. The first band contains predominantly low spin protein, and the second band contains predominantly high spin protein
T213A
-
the mutant enzyme shows an important red-shift of their fluorescence maximum, along with an increased shoulder at 396 nm, significant alteration in the protein structure, causing some of the tryptophan residues to become more solvent accessible
-
T213A/T214A
-
the mutant enzyme shows an important red-shift of their fluorescence maximum, along with an increased shoulder at 396 nm, significant alteration in the protein structure, causing some of the tryptophan residues to become more solvent accessible
-
T213W
-
the fluorescence yield of the T213W mutant enzyme is slightly lower than that of the wild type enzyme
-
T213A
-
formation of styrene epoxide is 83% compared to wild-type enzyme. Protein melting temperature is 1.6°C lower compared to wild-type enzyme
-
T213F
-
no formation of styrene epoxide. Protein melting temperature is 2.4°C lower compared to wild-type enzyme
-
T213S
-
formation of styrene epoxide is 19% compared to wild-type enzyme. Protein melting temperature is 2°C lower compared to wild-type enzyme
-
T213V
-
formation of styrene epoxide is 0.7% compared to wild-type enzyme. Protein melting temperature is 1.1°C lower compared to wild-type enzyme
-
T214A
-
formation of styrene epoxide is 2.7fold higher as compared to wild-type enzyme. Protein melting temperature is 1.6°C lower compared to wild-type enzyme
-
C61S
catalytically inactive
additional information