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Cellobiose dehydrogenase of Chaetomium sp. INBI 2‐26(–): Structural basis of enhanced activity toward glucose at neutral pH
Author(s) -
Vasilchenko Liliya G.,
Karapetyan Karen N.,
Yershevich Olga P.,
Ludwig Roland,
Zamocky Marcel,
Peterbauer Clemens K.,
Haltrich Dietmar,
Rabinovich Mikhail L.
Publication year - 2011
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201000373
Subject(s) - cellobiose dehydrogenase , cellobiose , biochemistry , dehydrogenase , thermophile , chemistry , amino acid , biology , enzyme , cellulase
Cellobiose dehydrogenase (CDH) is an extracellular fungal flavocytochrome specifically oxidizing cellooligosaccharides and lactose to corresponding (‐lactones by a variety of electron acceptors. In contrast to basidiomycetous CDHs, CDHs of ascomycetes also display certain activity toward glucose. The objective of this study was to establish the structural reasons of such an activity of CDH from mesophilic ascomycete Chaetomium sp. INBI 2‐26 ( Ch CDH). The complete amino acid sequence of Ch CDH displayed high levels of similarity with the amino acid sequences of CDHs from the thermophilic fungi Thielavia heterotallica and Myriococcum thermophilum. Peptide mass fingerprinting of purified Ch CDH provided evidence for the oxidation of methionine residues in the FAD‐domain. Comparative homology modeling of the structure of the Ch CDH FAD‐domain in complex with the transition state analog based on the structure of the same complex of basidiomycetous CDH (1NAA) as template indicated possible structural reasons for the enhanced activity of ascomycetous CDHs toward glucose at neutral pH, which is a prerequisite for application of CDH in a variety of biocompatible biosensors and biofuel cells.