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KMID : 0364820110470040302
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Korean Journal of Microbiology
2011 Volume.47 No. 4 p.302 ~ p.307
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Analysis of Amino Acid Residues Involved in Activities of Chitin Deacetylase of Aspergillus nidulans
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Kim Jong-II
Song Da-Hyun
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Abstract
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Native chitin deacetylase of Aspergillus nidulans was purified to apparent homogeneity by a combination of phenyl-Sepharose and Q-Sepharose column chromatography. In order to analyze the amino acid residues involved in the enzyme activity, the enzyme was chemically modified with chemical agent, which selectively reacted with the specific amino acid residue on the protein. When the enzyme was chemically modified with diethylpyrocarbonate, which specifically reacted with histidine residues on the protein, the activity was eliminated. The chitin deacetylase, chemically modified with 100 μM modifier at the residue of arginine or tyrosine, has shown to have decreased activities. It was shown that the modification at aspartic acid or glutamic acid did not affect the enzyme activity to a greater extent, which would not implicate that acid amino residues were directly involved in catalytic reaction and would affect on the global structures of the proteins. This results demonstrated that histidine and tyrosine residues of enzyme would participate in an important function of the chitin deacetylase activity.
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KEYWORD
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active residues, chitin deacetylase, coupled enzyme assay, site-specific chemical modification
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