ArticleThe Biochemical journal2000
Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 67 citations in OpenAlex.
- Ega3 from the fungal pathogenThe Journal of biological chemistry · 2019Article
- A mutation in an exoglucanase of Xanthomonas oryzae pv. oryzae, which confers an endo mode of activity, affects bacterial virulence, but not the induction of immune responses, in rice.Molecular plant pathology · 2018Article
- Advantages of a distant cellulase catalytic base.The Journal of biological chemistry · 2018Article
- The use of3 Biotech · 2018Article
- A Neutral Thermostable β-1,4-Glucanase from Humicola insolens Y1 with Potential for Applications in Various Industries.PloS one · 2015Article
- The three-dimensional structure of the cellobiohydrolase Cel7A from Aspergillus fumigatus at 1.5 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2015Article
- LenVarDB: database of length-variant protein domains.Nucleic acids research · 2014Article
- Loop motions important to product expulsion in the Thermobifida fusca glycoside hydrolase family 6 cellobiohydrolase from structural and computational studies.The Journal of biological chemistry · 2013Article
- Insights into exo- and endoglucanase activities of family 6 glycoside hydrolases from Podospora anserina.Applied and environmental microbiology · 2013Article
- Hallmarks of processivity in glycoside hydrolases from crystallographic and computational studies of the Serratia marcescens chitinases.The Journal of biological chemistry · 2012Article
- Crystallization and preliminary crystallographic studies of CbsA, a secretory exoglucanase from Xanthomonas oryzae pv. oryzae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Product binding varies dramatically between processive and nonprocessive cellulase enzymes.The Journal of biological chemistry · 2012Article
- Multiple functions of aromatic-carbohydrate interactions in a processive cellulase examined with molecular simulation.The Journal of biological chemistry · 2011Article
- Cellulases from thermophilic fungi: recent insights and biotechnological potential.Enzyme research · 2011Article
- Processivity, synergism, and substrate specificity of Thermobifida fusca Cel6B.Applied and environmental microbiology · 2009Article
- Heterologous expression, crystallization and preliminary X-ray characterization of CcCel6C, a glycoside hydrolase family 6 enzyme from the basidiomycete Coprinopsis cinerea.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Purification and characterization of a new family 45 endoglucanase, STCE1, from Staphylotrichum coccosporum and its overproduction in Humicola insolens.Applied and environmental microbiology · 2008Article
- Protein disorder: conformational distribution of the flexible linker in a chimeric double cellulase.Biophysical journal · 2005Article
- PFIT and PFRIT: bioinformatic algorithms for detecting glycosidase function from structure and sequence.Protein science : a publication of the Protein Society · 2004Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellulases are traditionally classified as either endoglucanases or cellobiohydrolases on the basis of their respective catalytic activities on crystalline cellulose, which is generally hydrolysed more efficiently only by the cellobiohydrolases. On the basis of the Trichoderma reesei cellobiohydrolase II structure, it was proposed that the active-site tunnel of cellobiohydrolases permitted the processive hydrolysis of cellulose, whereas the corresponding endoglucanases would display open active-site clefts [Rouvinen, Bergfors, Teeri, Knowles and Jones (1990) Science 249, 380-386]. Glycoside hydrolase family 6 contains both cellobiohydrolases and endoglucanases. The structure of the catalytic core of the family 6 endoglucanase Cel6B from Humicola insolens has been solved by molecular replacement with the known T. reesei cellobiohydrolase II as the search model. Strangely, at the sequence level, this enzyme exhibits the highest sequence similarity to family 6 cellobiohydrolases and displays just one of the loop deletions traditionally associated with endoglucanases in this family. However, this enzyme shows no activity on crystalline substrates but a high activity on soluble substrates, which is typical of an endoglucanase. The three-dimensional structure reveals that the deletion of just a single loop of the active site, coupled with the resultant conformational change in a second 'cellobiohydrolase-specific' loop, peels open the active-site tunnel to reveal a substrate-binding groove.
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10794732PMC1221054W1982946286What OpenQuestion holds
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