期刊论文详细信息
FEBS Letters
The primary structure of inhibitor of cysteine proteinases from potato
Drobnic̆-Kos̆orok, M.1  Brzin, J.1  Kriz̆aj, I.1  Turk, V.1  Jerala, R.1 
[1]Department of Biochemistry and Molecular Biology, Joz̆ef Stefan Institute, Jamova 39, 61111 Ljubljana, Slovenia
关键词: Cysteine proteinase inhibitor;    Amino acid sequence;    Solanum tuberosum;    Soybean trypsin inhibitor superfamily;    CPI;    cysteine proteinase inhibitor;    PCPI;    potato cysteine proteinase inhibitor;    MRC;    miraculin;    STI;    soybean trypsin inhibitor;    ETI;    Erythrina caffra trypsin inhibitor;    WASI;    wheat α-amylase/ proteinase K (subtilisin) inhibitor;    NID;    novel inhibitor of cathepsin D;    PP IV;    papaya proteinase IV;    CNBr;    cyanogen bromide;    CM-;    carboxymethyl-;    PE-;    pyridylethyl-;    HPLC;    high performance liquid chromatography;    3D;    threedimensional;   
DOI  :  10.1016/0014-5793(93)80366-3
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

The complete amino acid sequence of the cysteine proteinase inhibitor from potato tubers was determined. The inhibitor is a single-chain protein having 180 amino acid residues. Its primary structure was elucidated by automatic degradation of the intact protein and sequence analysis of peptides generated by CNBr, trypsin and glycyl endopeptidase. A search through the protein sequence database showed homology to other plant proteinase inhibitors of different specificities and non-inhibitory proteins of M r around 20,000. On the basis of sequence homology, prediction of secondary structure and fold compatibility, based on a 3D-1D score to the three-dimensional profile of Erythrina caffra trypsin inhibitor, we suggest that the potato cysteine proteinase inhibitor belongs to the superfamily of proteins that have the same pattern of three-dimensional structure as soybean trypsin inhibitor. This superfamily would therefore include proteins that inhibit three different classes of proteinases - serine, cysteine and aspartic proteinases.

【 授权许可】

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