Evidence map›Paper›PMID 18676702›Full record

ArticleApplied and environmental microbiology2008

Characterization of an endoglucanase belonging to a new subfamily of glycoside hydrolase family 45 of the basidiomycete Phanerochaete chrysosporium.

Kiyohiko Igarashi, Takuya Ishida, Chiaki Hori, Masahiro Samejima

Abstract read
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Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

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0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

34 citing papers in PubMed.

  1. Biomolecular NMR assignments · 2024
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  5. Genomic and Secretomic Analyses of the Newly Isolated FungusApplied and environmental microbiology · 2023
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  12. A Swollenin FromFrontiers in microbiology · 2021
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

4 authors.

Kiyohiko IgarashiDepartment of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo, Japan. amsam@mail.ecc.u-tokyo.ac.jp
Takuya Ishida
Chiaki Hori
Masahiro Samejima

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The wood decay fungus Phanerochaete chrysosporium has served as a model system for the study of lignocellulose conversions, but aspects of its cellulolytic system remain uncertain. Here, we report identifying the gene that encodes the glycoside hydrolase (GH) family 45 endoglucanase (EG) from the fungus, cloning the cDNA, determining its heterologous expression in the methylotrophic yeast Pichia pastoris, and characterizing the recombinant protein. The cDNA consisted of 718 bp, including an open reading frame encoding a 19-amino-acid signal peptide, a 7-amino-acid presequence at the N-terminal region, and a 180-amino-acid mature protein, which has no cellulose binding domain. Analysis of the amino acid sequence revealed that the protein has a low similarity (<22%) to known fungal EGs belonging to the GH family 45 (EGVs). No conserved domain of this family was found by a BLAST search, suggesting that the protein should be classified into a new subdivision of this GH family. The recombinant protein has hydrolytic activity toward amorphous cellulose, carboxylmethyl cellulose, lichenan, barley beta-glucan, and glucomannan but not xylan. Moreover, a synergistic effect was observed with the recombinant GH family 6 cellobiohydrolase from the same fungus toward amorphous cellulose as a substrate, indicating that the enzyme may act in concert with other cellulolytic enzymes to hydrolyze cellulosic biomass in nature.

Indexed as

Amino Acid SequenceCellulaseCloning, MolecularDNA, ComplementaryDNA, FungalFungal ProteinsGene ExpressionGenes, FungalGlycoside HydrolasesMolecular Sequence DataPhanerochaetePhylogenyRecombinant ProteinsReverse Transcriptase Polymerase Chain ReactionSequence AlignmentSubstrate SpecificityCellulaseDNA, ComplementaryDNA, FungalFungal ProteinsGlycoside HydrolasesRecombinant Proteins

Identifiers

PMID18676702
PMCPMC2547050

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.