6A6Q

Crystal structure of a lignin peroxidase isozyme H8 variant that is stable at very acidic pH

Summary for 6A6Q

• Entry DOI: 10.2210/pdb6a6q/pdb
• Descriptor: Ligninase H8, HEME B/C, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: peroxidase, oxidoreductase, heme binding domain
• Biological source: Phanerochaete chrysosporium RP-78 (White-rot fungus)
• Total number of polymer chains: 1
• Total formula weight: 38649.87

Authors

Seo, H.,Kim, K.-J.,Pham, L.T.M. (deposition date: 2018-06-29, release date: 2019-01-23, Last modification date: 2023-11-22)

Primary citation

Pham, L.T.M.,Seo, H.,Kim, K.J.,Kim, Y.H.
In silico-designed lignin peroxidase fromPhanerochaete chrysosporiumshows enhanced acid stability for depolymerization of lignin.
Biotechnol Biofuels, 11:325-325, 2018

PubMed Abstract: The lignin peroxidase isozyme H8 from the white-rot fungus (LiPH8) demonstrates a high redox potential and can efficiently catalyze the oxidation of veratryl alcohol, as well as the degradation of recalcitrant lignin. However, native LiPH8 is unstable under acidic pH conditions. This characteristic is a barrier to lignin depolymerization, as repolymerization of phenolic products occurs simultaneously at neutral pH. Because repolymerization of phenolics is repressed at acidic pH, a highly acid-stable LiPH8 could accelerate the selective depolymerization of recalcitrant lignin.

PubMed: 30555531
DOI: 10.1186/s13068-018-1324-4

Experimental method

X-RAY DIFFRACTION (1.67 Å)