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Lignin peroxidase crystal structures

Choinowski T, Blodig W, Winterhalter K et al (1999) The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxyl group on the Cb of tryptophan 171 A novel radical site formed during redox cycle. J Mol Biol 286 809-827... [Pg.58]

Piontek K, Glumoft T, Winterhalter K (1993) Low pH crystal structure of glycosylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 A resolution. FEBS Lett 315 119-124... [Pg.76]

Blodig W, Smith AT, WA D et al (2001) Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications on the reaction mechanism. J Mol Biol 305 851-861... [Pg.77]

Yeast cytochrome c peroxidase is carbohydrate-free the other three peroxidases are glycoproteins. Molecular weights are 35,200 for cytochrome c peroxidase, 40,000 for horseradish peroxidase, 41,000 for lignin peroxidase ", and 72,000 for prostaglandin H synthase. Die crystal structure of cytochrome c peroxidase has been determined ". ... [Pg.656]

Manganese peroxidase (MnP) is an unique enzyme in many respects. It is an extracellular enzyme that involves a heme protoporphyrin IX for the oxidation of Mn" to Mn " 94, 95). A crystal structure at 2.06-A resolution of the manganese peroxidase from the white rot basidiomycete Phanerocaete chrysosporium, which utilizes this enzyme to degrade lignin, appeared in 1994 96). The active site (Fig. 5) and the overall structure are quite similar to lignin peroxidase (LiP),... [Pg.315]


See other pages where Lignin peroxidase crystal structures is mentioned: [Pg.114]    [Pg.116]    [Pg.124]    [Pg.93]    [Pg.49]    [Pg.80]    [Pg.296]    [Pg.82]    [Pg.315]    [Pg.317]    [Pg.317]   
See also in sourсe #XX -- [ Pg.82 , Pg.83 , Pg.84 ]




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