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1.11.1.14: lignin peroxidase

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

Word Map on EC 1.11.1.14

Reaction

1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol
+
H2O2
=
3,4-dimethoxybenzaldehyde
+
2-methoxyphenol
+
glycolaldehyde
+
H2O

Synonyms

ALiP-P3, bacterial lignin peroxidase, diarylpropane oxygenase, diarylpropane peroxidase, diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving), DypB, fungal lignin peroxidase, Glg4, H2O2-dependent ligninase, heme-containing lignin peroxidase, heme-containing peroxidase, lignin peroxidase, lignin peroxidase H8, lignin peroxidase isozyme H8, lignin peroxidase LIII, ligninase, ligninase H2, ligninase H8, ligninase I, ligninase LG5, LIP, Lip1, LIP2, LiPH8, lipJ, LPA, LPOA, microbial lignin peroxidase, More, mushroom tyrosinase, oxygenase, diarylpropane, Pr-lip1, Pr-lip4

ECTree

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

Engineering

Engineering on EC 1.11.1.14 - lignin peroxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A140G/A243R/A317P
-
kcat/Km for 2,4-dichlorophenol is 4fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
A140G/S190P/P193A/S196F/E208Q
-
the variant shows increased 2,4-dichlorophenol degradation activity (ca. 1.6fold) and stability against H2O2. Kcat for H2O2 increases over the wild type value by about 6.5fold, the Km values for H2O2 is lower than wild type value
A55R/N156E/H239E
H102T/S119R/N120T/Q126K/A243R/A315G
-
kcat/Km for 2,4-dichlorophenol is fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
N182D/D183K/A36E
-
generating a Mn2+-binding site
P106R/Q210H/L211V/A243R/F255L
-
kcat/Km for 2,4-dichlorophenol is 4fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
P106R/S119R/N120T/S228Y/A272G/L275V/A315G/A317T
-
the variant shows increased 2,4-dichlorophenol degradation activity (ca. 1.6fold) and stability against H2O2. Kcat for H2O2 increases over the wild type value by about 6.5fold, the Km values for H2O2 is lower than wild type value
S274L/L275F/A292
-
the variant shows increased 2,4-dichlorophenol degradation activity (ca. 1.6fold) and stability against H2O2. Kcat for H2O2 increases over the wild type value by about 6.5fold, the Km values for H2O2 is lower than wild type value
S49C/A67C/H239E
site-directed mutagenesis, improved thermostability of the synthetic LiPH8 variant (PDB ID 6ISS) capable of strengthening the helix-loop interactions under acidic conditions. The mutant retains excellent thermostability at pH 2.5 with a 10fold increase in t1/2 (2.52 h at 25°C) compared with that of the wild-type enzyme. The recombinant LiPH8 variant is the only unique lignin peroxidase containing five disulfide bridges, and the helix-loop interactions of the synthetic disulfide bridge and ionic salt bridge in its structure are responsible for stabilizing the Ca2+-binding region and heme environment, resulting in an increase in overall structural resistance against acidic conditions
W171F
-
no activity towards veratryl alcohol
N246A
site-directed mutagenesis, mutant Rh_DypB
additional information