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Essential carboxy groups in xylanase A.

M R Bray1, A J Clarke

  • 1Department of Microbiology, University of Guelph, Ontario, Canada.

The Biochemical Journal
|August 15, 1990
PubMed
Summary
This summary is machine-generated.

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Carboxyl groups are crucial for Schizophyllum commune endo-1,4-beta-xylanase activity, as shown by chemical modification studies. Protecting these groups with xylo-oligomers maintains enzyme function.

Area of Science:

  • Enzymology
  • Biochemistry
  • Protein Chemistry

Background:

  • Schizophyllum commune produces endo-1,4-beta-xylanase, an enzyme vital for breaking down xylan.
  • Understanding the enzyme's catalytic mechanism is essential for its biotechnological applications.

Purpose of the Study:

  • To investigate the role of carboxyl groups in the catalytic mechanism of endo-1,4-beta-xylanase from Schizophyllum commune.
  • To identify critical amino acid residues involved in enzyme activity.

Main Methods:

  • Purification of endo-1,4-beta-xylanase using DEAE-Sepharose CL-6B and Sephadex G-50 chromatography.
  • Chemical modification studies using carbodi-imides (EAC), diethyl pyrocarbonate, tetranitromethane, and thiol-reactive reagents.
  • Enzyme activity assays and pH-dependence studies.

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Main Results:

  • 1-(4-azonia-4,4-dimethylpentyl)-3-ethylcarbodi-imide iodide (EAC) rapidly inactivated the xylanase, indicating the importance of carboxyl groups.
  • Xylo-oligomers protected the enzyme from EAC inactivation, suggesting their role in substrate binding.
  • A critical ionizable group with a pKa of 6.6 was identified in the active site.
  • Histidine, thiol, and tyrosine residues were found not to be essential for catalytic activity.

Conclusions:

  • Carboxyl groups are essential for the catalytic activity of Schizophyllum commune endo-1,4-beta-xylanase.
  • The enzyme's active site contains a critical ionizable group with a pKa of 6.6.
  • Chemical modification studies provide insights into the enzyme's catalytic mechanism and active site residues.