Complete amino acid sequence of chitinase-a from bulbs of gladiolus (Gladiolus gandavensis).
The complete amino acid sequence of gladiolus bulb chitinase-a (GBC-a) was determined. First the tryptic peptides from GBC-a after it was reduced and S-carboxymethylated were sequenced and then the peptides were further studied by chemical cleavage of the enzyme. GBC-a consisted of 274 amino acid residues and had a molecular mass of 30,714 Da. Two consensus sequences essential for chitinase activity by plant class III chitinases were conserved in GBC-a, although its sequence similarity with plant class III chitinases was less than 20%. Sequence comparison of GBC-a with sequences of other proteins in a protein identification resource (PIR) showed that the GBC-a sequence was 33% similar to that of narbonin, a seed storage 2S globulin from narbon beans.
Yamagami
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Laboratory of Protein Chemistry & Engineering, Faculty of Agriculture, Kyushu University, Fukuoka, Japan. yamagami@agr.kyushu-u.ac.jp
Mine
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Y
Ishiguro
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D000595:Amino Acid Sequence; D002688:Chitinases / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000737:chemistry; D010450:Endopeptidases / Q000737:chemistry; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D018517:Plant Roots / Q000201:enzymology; D010944:Plants / Q000201:enzymology*; D016415:Sequence Alignment; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D014357:Trypsin / Q000737:chemistry
D002688:Chitinases; D010450:Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin; D008666:Metalloendopeptidases; C058921:endoproteinase Asp-N