Ritch T G, Nipper V J, Akileswaran L, Smith A J, Pribnow D G, Gold M H
Department of Chemical and Biological Sciences, Oregon Graduate Institute for Science and Technology, Beaverton 97006-1999.
Gene. 1991 Oct 30;107(1):119-26. doi: 10.1016/0378-1119(91)90304-t.
The cDNA clone L18 encoding lignin peroxidase LiP2, the most highly expressed LiP isozyme from Phanerochaete chrysosporium strain OGC101, was isolated and sequenced. Comparison of the cDNA sequence with the N-terminal sequence of the mature LiP2 protein isolated from culture medium suggests that the mature protein contains 343 amino acids (aa) and is preceded by a 28-aa leader sequence. In vitro transcription followed by in vitro translation and processing by signal peptidase resulted in cleavage at a site following the Ala21 (counted from the N-terminal Met1 of the initial translation product). The resultant protein contains a 7-aa propeptide, indicating that LiP is synthesized as a preproenzyme.
