The Amino Acid Sequence of Monal Pheasant Lysozyme and Its Activity | Zendy

Tomohiro ARAKI | Zendy; Takako MATSUMOTO | Zendy; Takao Torikata | Zendy

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The Amino Acid Sequence of Monal Pheasant Lysozyme and Its Activity

Author(s) -

Tomohiro ARAKI,

Takako MATSUMOTO,

Takao Torikata

Publication year - 1998

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.62.1988

Subject(s) - lysozyme , amino acid , pheasant , peptide sequence , chemistry , trypsin , pentamer , biochemistry , stereochemistry , biology , enzyme , gene , paleontology

The amino acid sequence of monal pheasant lysozyme and its activity were analyzed. Carboxymethylated lysozyme was digested with trypsin and the resulting peptides were sequenced. The established amino acid sequence had one amino acid substitution at position 102 (Arg to Gly) comparing with Indian peafowl lysozyme and four amino acid substitutions at positions 3 (Phe to Tyr), 15 (His to Leu), 41 (Gln to His), and 121 (Gln to His) with chicken lysozyme. Analysis of the time-courses of reaction using N-acetylglucosamine pentamer as a substrate showed a difference of binding free energy change (-0.4 kcal/mol) at subsites A between monal pheasant and Indian peafowl lysozyme. This was assumed to be caused by the amino acid substitution at subsite A with loss of a positive charge at position 102 (Arg102 to Gly).

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