The complete amino acid sequence of chitinase-c from the seeds of rye (Secale cereal).
The complete amino acid sequence of rye seed chitinase-c (RSC-c) has been analyzed. This was done by first sequencing the tryptic peptides from RCm-RSC-c and then connecting them by analyzing the peptides produced by digestions with lysylendopeptidase and Staphylococcus aureus V8 protease of RCm-RSC-c, and by chymotryptic digestion and formic acid cleavage of S. aureus V8 protease peptides. RSC-c consists of 243 amino acid residues and has a molecular mass of 26,093, and has 92% sequence homology with barley seed basic chitinase which lacks a Cys-rich domain. Cys204 is free and six cysteine residues are linked by disulfide bonds between Cys23 and Cys85, Cys97 and Cys105, and Cys223 and Cys236.
Yamagami
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Laboratory of Protein Chemistry & Engineering, Faculty of Agriculture, Kyusyu University, Fukuoka, Japan.
Funatsu
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002688:Chitinases / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism; D005561:Formates / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D012434:Secale / Q000201:enzymology*; D012639:Seeds / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid
D000596:Amino Acids; D005561:Formates; D010446:Peptide Fragments; C030544:formic acid; D002688:Chitinases; D010450:Endopeptidases