BIOMAT Database Logo BIOMAT Database Logo

Chemical replacement of P1' arginine residue at the first reactive site of peanut protease inhibitor B-III. 1987

T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka

The contribution of the P1' residue at the first reactive site of peanut protease inhibitor B-III to the inhibition was analyzed by replacement of the P1' Arg(11) with other amino acids (Arg, Ser, Ala, Leu, Phe, Asp) after selective modification of the second reactive site. The Arg derivative had the same trypsin inhibitory activity as the native inhibitor (Ki = 2 X 10(-9) M). The Ser derivative inhibited more weakly (Ki = 2 X 10(-8) M). The Ala and Leu derivatives inhibited trypsin very weakly (Ki = 2 X 10(-7) M and 4 X 10(-7) M, respectively), and the Phe and Asp derivatives not at all. These results suggest that the P1' arginine residue is best for inhibitory activity at the first reactive site of B-III, although it has been suggested that a P1' serine residue at the reactive site is best for inhibitory activity of Bowman-Birk type inhibitors.

UI MeSH Term Description Entries
D010940 Plant Proteins Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available. Plant Protein,Protein, Plant,Proteins, Plant
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D001120 Arginine An essential amino acid that is physiologically active in the L-form. Arginine Hydrochloride,Arginine, L-Isomer,DL-Arginine Acetate, Monohydrate,L-Arginine,Arginine, L Isomer,DL Arginine Acetate, Monohydrate,Hydrochloride, Arginine,L Arginine,L-Isomer Arginine,Monohydrate DL-Arginine Acetate
D013329 Structure-Activity Relationship The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups. Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D014357 Trypsin A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. Tripcellim,Trypure,beta-Trypsin,beta Trypsin
D014361 Trypsin Inhibitors Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds. Trypsin Inhibitor,Inhibitor, Trypsin,Inhibitors, Trypsin

Related Publications

T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka
A subtilisin inhibitor produced by Streptomyces bikiniensis possesses a glutamine residue at reactive site P1.
March 1995, Journal of biochemistry,
T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka
Examples of peptide-peptoid hybrid serine protease inhibitors based on the trypsin inhibitor SFTI-1 with complete protease resistance at the P1-P1' reactive site.
June 2005, Chembiochem : a European journal of chemical biology,
T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka
Participation of S-S loops in inhibitory activity of peanut protease inhibitor B-III.
March 1987, Journal of biochemistry,
T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka
Exploration of the P1 residue in 3CL protease inhibitors leading to the discovery of a 2-tetrahydrofuran P1 replacement.
February 2024, Bioorganic & medicinal chemistry,
T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka
Chemical-enzymatic replacement of Ile64 in the reactive site of soybeen trypsin inhibitor (Kunitz).
March 1976, Biochemistry,
T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka
Enzymatic replacement of the arginyl by a lysyl residue in the reactive site of soybean trypsin inhibitor.
September 1969, Biochemistry,
T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka
Chemical-enzymatic insertion of an amino acid residue in the reactive site of soybean trypsin inhibitor (Kunitz).
March 1976, Biochemistry,
T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka
Replacement of lysine by arginine, phenylalanine, and tryptophan in the reactive site of the trypsin-kallikrein inhibitor (Kunitz).
October 1974, Angewandte Chemie (International ed. in English),
T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka
Synthesis of an elastase inhibitor by monosubstitution of arginine-5 with valine at the reactive site in a trypsin inhibitor from squash seeds (CMTI III).
May 1989, Biological chemistry Hoppe-Seyler,
T Kurokawa, and S Hara, and S Norioka, and T Teshima, and T Ikenaka
Chemical evidence for a functional arginine residue in carboxypeptidase B.
July 1972, Biochemical and biophysical research communications,
Copied contents to your clipboard!