PMID: 2119305Aug 28, 1990Paper

Kinetics and specificities of two closely related beta-glucosidases secreted by Schizophyllum commune

European Journal of Biochemistry
A C LoG E Willick

Abstract

Two beta-glucosidases (I and II) were isolated from Schizophyllum commune, and their physical and chemical properties studied. The two enzymes have very similar sequences, as shown by HPLC analysis of tryptic digests and partial amino acid sequencing. As judged by their circular dichroism spectra, they have almost identical secondary structure. The estimates for alpha-helix, beta-sheet, and other structures were 21%, 40% and 39%, respectively, for beta-glucosidase I and 27%, 32% and 41% for beta-glucosidase II. Their near-ultraviolet spectra were identical. beta-Glucosidase I was more highly glycosylated than beta-glucosidase II, having 2 mol N-acetylglucosamine/mol enzyme 36, mol mannose/mol enzyme and 1.2 mol glucose/mol enzyme vs 1.2, 17 and 3 mol/mol, respectively, in beta-glucosidase II. The native glycosylated form of beta-glucosidase I had a molecular mass of 102 kDa, and that of beta-glucosidase II, 96 kDa. As estimated from sensitivity to N-glycanase, beta-glucosidase II sugars were mainly asparagine linked, but much of the sugar in beta-glucosidase I was not removed by this treatment and was apparently serine or threonine linked. Kinetic analysis showed that both forms had similar Km values (0.3-2.1 mM) for oligosacch...Continue Reading

References

Jan 1, 1979·Methods in Enzymology·K F Tipton, H B Dixon
Oct 1, 1977·Analytical Biochemistry·A J Mort, D T Lamport
Sep 11, 1985·Nucleic Acids Research·C Kohchi, A Toh-e
Mar 1, 1981·Archives of Biochemistry and Biophysics·J G Shewale, J Sadana
Jan 6, 1981·Biochemistry·S W Provencher, J Glöckner

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Citations

Feb 16, 2013·Enzyme and Microbial Technology·Nongnuch SutivisedsakStephen W Peterson
Nov 28, 2014·Microbiology and Molecular Biology Reviews : MMBR·Johanna RytiojaMiia R Mäkelä

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