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Literature summary for 1.11.1.14 extracted from

  • Son, H.; Seo, H.; Han, S.; Kim, S.M.; Pham, L.T.M.; Khan, M.F.; Sung, H.J.; Kang, S.H.; Kim, K.J.; Kim, Y.H.
    Extra disulfide and ionic salt bridge improves the thermostability of lignin peroxidase H8 under acidic condition (2021), Enzyme Microb. Technol., 148, 109803 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information improving the thermostability of LiP in acidic environments is required for effective lignin depolymerization in practical applications Phanerodontia chrysosporium
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 Phanerodontia chrysosporium

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium P06181
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Synonyms

Synonyms Comment Organism
lignin peroxidase
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Phanerodontia chrysosporium
lignin peroxidase H8
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Phanerodontia chrysosporium
LIP
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Phanerodontia chrysosporium
LiPH8
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Phanerodontia chrysosporium

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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an extra disulfide and ionic salt bridge improves the thermostability of lignin peroxidase H8 under acidic condition. Native LiP under mild conditions with half-life (t1/2) of 8.2 days at pH 6.0 exhibits a marked decline in thermostability under acidic conditions with t1/2 of only 14 min at pH 2.5 Phanerodontia chrysosporium

Cofactor

Cofactor Comment Organism Structure
heme
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Phanerodontia chrysosporium