Literature summary for 1.11.1.14 extracted from

Ecker, J.; Fueloep, L.
Lignin peroxidase ligand access channel dysfunction in the presence of atrazine (2018), Sci. Rep., 8, 5989 .

Search for more literature for 1.11.1.14

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	each subunit of the homodimeric enzyme contains two Ca2+ ion binding sites	Phanerodontia chrysosporium

Organism

Organism	UniProt	Comment	Textmining
Phanerodontia chrysosporium	-	-	-

Subunits

Subunits	Comment	Organism
homodimer	-	Phanerodontia chrysosporium

Synonyms

Synonyms	Comment	Organism
lignin peroxidase	-	Phanerodontia chrysosporium

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Phanerodontia chrysosporium

General Information

General Information	Comment	Organism
additional information	lignin peroxidase is unable to degrade atrazine, analysis of the connection between the structural and dynamical properties of the enzyme and its incapability to degrade atrazine, protein-ligand docking and molecular dynamics study, three-dimensional modeling of the lignin peroxidase-atrazine complex, overview. Atrazine has no access to heme edge due to the electric charges of the delocalized S-triazine ring. The detected phenomenon suggests that the small size of the ligands only is not a sufficient condition to access the active site. Their physicochemical properties also influence the structural behaviour of the channel. The lignin peroxidase can directly oxidize lignin in the partially degraded plant cell walls cannot be excluded. Lignin peroxidase has a so-called ligand access channel which allows direct interaction between the substrate and the heme. Residues His82, Ile85, Glu146, Phe148, Asp183, Val184 and Gln222 are located in this channel. The channel is sterically restricted and does not allow access to large bulky (lignin) substrates. The enzyme's natural substrate, veratrol, can easily approach heme through the ligand access channel. Based on the results of protein-ligand docking, atrazine can find an energetically favourable position in the environment of the ligand channel residues, although, the mathematical probability of the formation of these complexes is not significant (10%, 16% and 53% frequency values at three different temperatures)	Phanerodontia chrysosporium

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)