Identification of the Aspartic Acid Residue Located at or near Substrate-binding Site of Rye Seed Chitinase-c

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概要

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• Carboxyl groups of rye seed chitinase-c (RSC-c) were modified with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and glycine ethyl ester (GEE) at pH5.5 and 5°C in the presence and absence of (GlcNAc)_4. In the absence of (GlcNAc)_4, 5.2 carboxyl groups were modified by 90 min-reaction and the chitinase activity was reduced to 2.0%, while in the presence of (GlcNAc)_4, 4.6 carboxyl groups were modified and 72% of the activity was retained. To identify the carboxyl group protected by (GlcNAc)_4 from the modification, RSC-c was first modified with EDC and GEE in the presence of (GlcNAc)_4 and then radiolabeled with EDC and [^14C]GEE in the absence of (GlcNAc)_4. Analyses of the radioactive peptides from the tryptic and chymotryptic digests of radiolabeled RSC-c showed that the main radiolabeled carboxyl group is that of Asp95, suggesting that Asp95 is located at or near substrate-binding site of RSC-c.

• 社団法人日本農芸化学会の論文
• 1998-02-23

著者

• Funatsu Gunki

  Laboratory Of Biochemistry And ** Laboratory Of Protein Chemistry & Engineering Faculty Of Agric

• YAMAGAMI Takeshi

  Laboratories of Protein Chemistry and Engineering

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