Amino-acid sequence of a trypsin/chymotrypsin inhibitor from giant taro (Alocasiamacrorrhiza)
| Autor: | Denis C. Shaw, Argall Me, J H Bradbury |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Molecular Sequence Data
Biophysics Biochemistry Structural Biology medicine Chymotrypsin Amino Acid Sequence Molecular Biology Peptide sequence Plant Proteins chemistry.chemical_classification biology Kunitz STI protease inhibitor Subtilisin Trypsin Molecular biology Enzyme chemistry Enzyme inhibitor Neutrophil elastase biology.protein Trypsin Inhibitors Sequence Alignment medicine.drug |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1204:189-194 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/0167-4838(94)90008-6 |
| Popis: | Giant taro (Alocasiamacrorrhiza) contains a protein which inhibits both trypsin and chymotrypsin. This trypsin/chymotrypsin inhibitor exists as a dimer of two identical monomers each with slight polymorphism and is an attractive candidate for conferring insect resistance in transgenic plants. The 184 amino-acid sequence (molecular mass of 19774 Da for the Met-24, Glu-50 form) has been determined and is compared with those of other Kunitz-type trypsin, chymotrypsin and subtilisin inhibitors. There appears to be greater ‘homology’ between the giant taro inhibitor and those inhibitors from other monocotyledons than inhibitors from dicotyledons. The P1 loop region is different from that of other Kunitz-type inhibitors and contains a sequence Leu-Ala-Phe-Phe-Pro at residues 56–60. This section of sequence differs only by a Leu/Ile replacement to a tight binding inhibitor of neutrophil elastase, Recently produced by genetic engineering. The most likely candidate for the P1 residue in the giant taro trypsin/chymotrypsin inhibitor is Leu-56. |
| Databáze: | OpenAIRE |
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