Lignin peroxidase

From Proteopedia

Revision as of 10:01, 31 August 2020

spinqualitylabelsall models Lignin peroxidase containing heme complex with MPD, Ca+2 (large green), Na+ (purple) and Cl- (small green) ions (PDB entry 3q3u) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Lignin peroxidase or ligninase (Lip) catalyzes the biodegradation of lignin using hydrogen peroxide. Lignin comprises 20-30% of woody plants cell wall. It is made of branched and heterogenous structure of phenylpropanoid units. It is highly resistant to biodegradation and only higher fungi are capable of degrading it. Veratryl alcohol is the cofactor in this reaction[1]. Relevance Lip is used as a skin-lightening active agent[2]. Structural highlights . Water molecules are shown as red spheres. . . . .

3D structures of lignin peroxidase

Updated on 31-August-2020

1lga, 1llp, 1qpa, 1b80, 1b82 – PcLip – Phanerochaete chrysosporium
1b85, 6a6q, 6iss – PcLip (mutant)
3q3u – Lip – Trametes cervina

References

1. ↑ Doyle WA, Blodig W, Veitch NC, Piontek K, Smith AT. Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis. Biochemistry. 1998 Oct 27;37(43):15097-105. PMID:9790672 doi:http://dx.doi.org/10.1021/bi981633h
2. ↑ Zhong SM, Sun N, Liu HX, Niu YQ, Wu Y. Reduction of facial pigmentation of melasma by topical lignin peroxidase: A novel fast-acting skin-lightening agent. Exp Ther Med. 2015 Feb;9(2):341-344. Epub 2014 Dec 8. PMID:25574195 doi:http://dx.doi.org/10.3892/etm.2014.2118