| escherichia coli expression and in vitro activation of a unique ligninolytic peroxidase that has a catalytic tyrosine residue. | heterologous expression of trametes cervina lignin peroxidase (lip), the only basidiomycete peroxidase that has a catalytic tyrosine, was investigated. the mature lip cdna was cloned into the pet vector and used to transform escherichia coli. recombinant lip protein accumulated in inclusion bodies as an inactive form. refolding conditions for its in vitro activation-including incorporation of heme and structural ca2+ ions, and formation of disulfide bridges-were optimized taking as a starting po ... | 2009 | 19505579 |
| molecular characterization of lignin peroxidase from the white-rot basidiomycete trametes cervina: a novel fungal peroxidase. | the lignin peroxidase (lip) from trametes cervina was cloned, characterized, and identified as a novel fungal peroxidase. the sequence of t. cervina lip encodes the essential amino acids for shaping the heme cavity and calcium-binding sites, which are conserved in plant and fungal peroxidases. however, a sequence homology analysis showed that t. cervina lip has two unique features: it lacks the conserved tryptophan residue corresponding to the substrate-oxidation site (trp171) of phanerochaete c ... | 2010 | 20070371 |
| crystallographic, kinetic, and spectroscopic study of the first ligninolytic peroxidase presenting a catalytic tyrosine. | trametes cervina lignin peroxidase (lip) is a unique enzyme lacking the catalytic tryptophan strictly conserved in all other lips and versatile peroxidases (more than 30 sequences available). recombinant t. cervina lip and site-directed variants were investigated by crystallographic, kinetic, and spectroscopic techniques. the crystal structure shows three substrate oxidation site candidates involving his-170, asp-146, and tyr-181. steady-state kinetics for oxidation of veratryl alcohol (the typi ... | 2011 | 21367853 |
| determination of a catalytic tyrosine in trametes cervina lignin peroxidase with chemical modification techniques. | trametes cervina lignin peroxidase (lip) lacks a catalytic tryptophan strictly conserved in other lip and versatile peroxidases. it contains tyrosine(181) at the potential catalytic site. this protein and the well-characterized phanerochaete chrysosporium lip with the catalytic tryptophan(171) have been chemically modified: the tryptophan-specific modification with n-bromosuccinimide sufficiently disrupted oxidation of veratryl alcohol by p. chrysosporium lip, whereas the activity of t. cervina ... | 2011 | 21373922 |