Complete amino acid sequences of chitinase-1 and -2 from bulbs of genus Tulipa.
The complete amino acid sequences of tulip bulb chitinase-1 and -2 (TBC-1 and -2) were determined. The sequences of the TBC-1 and TBC-2 were solved by analysis of peptides derived by enzymatic digestions as well as by chemical cleavages with cyanogen bromide (CNBr), o-iodosobenzoic acid, and hydroxylamine. TBC-1 and TBC-2 both consisted of 275 amino acid residues and had molecular masses of 30,825 and 30,863, respectively. They shared 247 identical residues, that is 90% identity. Comparison of their sequences with that of gladiolus bulb class IIIb chitinase-a (GBC-a) showed that 63% of the residues of both TBC-1 and TBC-2 are identical to that of GBC-a. From these results, it was seen that TBC-1 and -2 are class IIIb chitinases. The characteristic difference in specific activity between TBC-1 and -2 was also discussed on the basis of their amino acid sequences.
Yamagami
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Laboratory of Protein Chemistry and Engineering, Faculty of Agriculture, Kyushu University, Fukuoka, Japan. yamagami@agr.kyushu-u_ac.jp
Ishiguro
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D000595:Amino Acid Sequence; D002688:Chitinases / Q000737:chemistry*; D003488:Cyanogen Bromide; D007527:Isoenzymes / Q000737:chemistry*; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D013438:Sulfhydryl Compounds / Q000032:analysis; D017186:Titrimetry
D007527:Isoenzymes; D013438:Sulfhydryl Compounds; D002688:Chitinases; D003488:Cyanogen Bromide