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Publication Abstract from PubMed

A crystal structure of banyan peroxidase (BP) purified from the latex of Ficus benghalensis, has been solved at 1.67 A resolution by SAD phasing. The refined structure includes 306 amino acid residues, a heme, and two calcium ions. The protein belongs to class III peroxidases and is the first one from plant latex. Extensive glycosylation was observed with N-linked glycans attached to seven asparagine residues. The enzyme is stable against a wide range of pH, temperature, chemical denaturants and organic solvents probably due to its high glycosylation. An unexpected post-translational modification of Asp290 was identified as succinimide moiety. Kinetic parameters of BP have been determined using various hydrogen donor substrates and hydrogen peroxide. This article is protected by copyright. All rights reserved.

Posttranslational modification and extended glycosylation pattern of a plant latex peroxidase of native source characterized by X-ray crystallography.,Palm GJ, Sharma A, Kumari M, Panjikar S, Albrecht D, Jagannadham MV, Hinrichs W FEBS J. 2014 Jun 30. doi: 10.1111/febs.12900. PMID:24980207^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.