Addition of Veratryl Alcohol Oxidase Activity to Manganese Peroxidase by Site-Directed Mutagenesis

1999 ◽  
Vol 256 (3) ◽  
pp. 500-504 ◽  
Author(s):  
Sergei L. Timofeevski ◽  
Guojun Nie ◽  
N.Scott Reading ◽  
Steven D. Aust
Keyword(s):  
Manganese Peroxidase ◽  
Oxidase Activity ◽  
Alcohol Oxidase ◽  
Veratryl Alcohol ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Veratryl Alcohol Oxidase

Inhibition of veratryl alcohol oxidase activity of lignin peroxidase H2 by 3-amino-1,2,4-triazole

1992 ◽  
Vol 293 (2) ◽  
pp. 287-291 ◽  
Author(s):  
Helfried Tuisel ◽  
Thomas A. Grover ◽  
John A. Bumpus ◽  
Steven D. Aust
Keyword(s):  
Lignin Peroxidase ◽  
Oxidase Activity ◽  
Alcohol Oxidase ◽  
Veratryl Alcohol ◽  
Veratryl Alcohol Oxidase

scholarly journals Site-directed mutagenesis of selected residues at the active site of aryl-alcohol oxidase, an H2O2-producing ligninolytic enzyme

FEBS Journal ◽  
2006 ◽  
Vol 273 (21) ◽  
pp. 4878-4888 ◽  
Author(s):  
Patricia Ferreira ◽  
Francisco J. Ruiz-Dueñas ◽  
María J. Martínez ◽  
Willem J. H. van Berkel ◽  
Angel T. Martínez
Keyword(s):  
Active Site ◽  
Alcohol Oxidase ◽  
Ligninolytic Enzyme ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

scholarly journals Structural implications of the C-terminal tail in the catalytic and stability properties of manganese peroxidases from ligninolytic fungi

2014 ◽  
Vol 70 (12) ◽  
pp. 3253-3265 ◽  
Author(s):  
Elena Fernández-Fueyo ◽  
Sandra Acebes ◽  
Francisco J. Ruiz-Dueñas ◽  
María Jesús Martínez ◽  
Antonio Romero ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Electron Transfer ◽  
Manganese Peroxidase ◽  
Catalytic Properties ◽  
Substrate Oxidation ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Ceriporiopsis Subvermispora ◽  
Ligninolytic Fungi ◽  
Access Channel

The genome ofCeriporiopsis subvermisporaincludes 13 manganese peroxidase (MnP) genes representative of the three subfamilies described in ligninolytic fungi, which share an Mn2+-oxidation site and have varying lengths of the C-terminal tail. Short, long and extralong MnPs were heterologously expressed and biochemically characterized, and the first structure of an extralong MnP was solved. Its C-terminal tail surrounds the haem-propionate access channel, contributing to Mn2+oxidation by the internal propionate, but prevents the oxidation of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS), which is only oxidized by short MnPs and by shortened-tail variants from site-directed mutagenesis. The tail, which is anchored by numerous contacts, not only affects the catalytic properties of long/extralong MnPs but is also associated with their high acidic stability. Cd2+binds at the Mn2+-oxidation site and competitively inhibits oxidation of both Mn2+and ABTS. Moreover, mutations blocking the haem-propionate channel prevent substrate oxidation. This agrees with molecular simulations that position ABTS at an electron-transfer distance from the haem propionates of anin silicoshortened-tail form, while it cannot reach this position in the extralong MnP crystal structure. Only small differences exist between the long and the extralong MnPs, which do not justify their classification as two different subfamilies, but they significantly differ from the short MnPs, with the presence/absence of the C-terminal tail extension being implicated in these differences.

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