6A6Q

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

6A6Q の概要

• エントリーDOI: 10.2210/pdb6a6q/pdb
• 分子名称: Ligninase H8, HEME B/C, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: peroxidase, oxidoreductase, heme binding domain
• 由来する生物種: Phanerochaete chrysosporium RP-78 (White-rot fungus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38649.87

構造登録者

Seo, H.,Kim, K.-J.,Pham, L.T.M. (登録日: 2018-06-29, 公開日: 2019-01-23, 最終更新日: 2023-11-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.67 Å)