ArticleThe Biochemical journal1996
Substrate specificity of endoglucanase A from Cellulomonas fimi: fundamental differences between endoglucanases and exoglucanases from family 6.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 47 citations in OpenAlex.
- Chitin-Active Lytic Polysaccharide Monooxygenases Are Rare inApplied and environmental microbiology · 2022Article
- Synergistic hydrolysis of filter paper by recombinant cellulase cocktails leveraging a key cellobiase, Cba2, ofFrontiers in bioengineering and biotechnology · 2022Article
- Four cellulose-active lytic polysaccharide monooxygenases from Cellulomonas species.Biotechnology for biofuels · 2021Article
- A complex gene locus enables xyloglucan utilization in the model saprophyte Cellvibrio japonicus.Molecular microbiology · 2014Article
- MALDI-TOF MS analysis of cellodextrins and xylo-oligosaccharides produced by hindgut homogenates of Reticulitermes santonensis.Molecules (Basel, Switzerland) · 2014Article
- Computational investigation of the pH dependence of loop flexibility and catalytic function in glycoside hydrolases.The Journal of biological chemistry · 2013Article
- A new sialidase mechanism: bacteriophage K1F endo-sialidase is an inverting glycosidase.The Journal of biological chemistry · 2009Article
- Incorporation of fungal cellulases in bacterial minicellulosomes yields viable, synergistically acting cellulolytic complexes.Applied and environmental microbiology · 2007Article
- Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution.The Biochemical journal · 2000Article
- Hydrolyses of alpha- and beta-cellobiosyl fluorides by Cel6A (cellobiohydrolase II) of Trichoderma reesei and Humicola insolens.The Biochemical journal · 2000Article
- Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution.The Biochemical journal · 1999Article
- Analysis of molecular size distributions of cellulose molecules during hydrolysis of cellulose by recombinant Cellulomonas fimi beta-1,4-glucanases.Applied and environmental microbiology · 1998Article
- Intrinsic fluorescence in endoglucanase and cellobiohydrolase from Trichoderma pseudokiningii S-38: effects of pH, quenching agents, and ligand binding.Journal of protein chemistry · 1997Article
- Circular dichroism studies in conformation of cellobiohydrolase and endoglucanase from Trichoderma pseudokiningii S-38: effects of pH and ligand binding.Journal of protein chemistry · 1997Article
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Values of kcat. and Km for the hydrolysis of cellotetraose, cellotriose, beta-cellobiosyl fluoride and various beta-aryl cellobiosides by endoglucanase A (CenA) from Cellulomonas fimi indicate that specific binding interactions between the reducing-end glucose residues of cellotetraose and cellotriose and the enzyme at the transition state provide enormous stabilization, endowing glucose with the "effective leaving group ability' of 2,4-dinitrophenol. As has been seen with several other inverting glycosidases, CenA hydrolyses the "wrong' anomer of its glycosyl fluoride substrate, alpha-cellobiosyl fluoride, according to non-Michaelian kinetics. This indicates that CenA carries out this hydrolysis by a mechanism involving binding of two substrate molecules in the active site (Hehre, Brewer and Genghof (1979) J. Biol. Chem. 254, 5942-5950] in contrast with that reported for cellobiohydrolase II, another family-6 enzyme [Konstantinidis, Marsden and Sinnott (1993) Biochem. J. 291, 833-838]. The pH profiles for wild-type CenA indicate that kcat. for CenA depends on the presence of both a protonated group and a deprotonated group for full activity, consistent with the presence of an acid and a base catalyst at the active site. By contrast, the profile for the Asp252Ala mutant of CenA shows a dependence only on a base-catalytic group, thereby confirming the role of Asp-252 as an acid catalyst. These results show that hydrolysis by CenA occurs by a typical inverting mechanism involving both acid and base catalysis, as first proposed by Koshland. It also suggests that endoglucanases from family 6 may function by fundamentally different mechanisms for exoglucanases in this family.
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