Positions of disulfide bonds in rye (Secale cereale) seed chitinase-a.
The positions of disulfide bonds of rye seed chitinase-a (RSC-a) were identified by the isolation of disulfide-containing peptides produced with enzymatic and/or chemical cleavages of RSC-a, followed by sequencing them. An unequivocal assignment of disulfide bonds in this enzyme was as follows: Cys3-Cysl8, Cys12-Cys24, Cys15-Cys42, Cys17-Cys31, and Cys35-Cys39 in the chitin-binding domain (CB domain), Cys82-Cys144, Cys156-Cys164, and Cys282-Cys295 in the catalytic domain (Cat domain), and Cys263 was a free form.
Laboratory of Protein Chemistry and Engineering, Faculty of Agriculture, Kyushu University, Fukuoka, Japan. yamagami@agr.kyushu-u.ac.jp
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Yamagami
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Funatsu
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Ishiguro
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D020134:Catalytic Domain; D002688:Chitinases / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D004220:Disulfides / Q000737:chemistry; D008969:Molecular Sequence Data; D012434:Secale / Q000201:enzymology* / Q000235:genetics; D012639:Seeds / Q000201:enzymology; D017386:Sequence Homology, Amino Acid
D000596:Amino Acids; D004220:Disulfides; D002688:Chitinases