A novel subclassification for Kunitz proteinase inhibitors from leguminous seeds.
Kunitz-type trypsin inhibitors from legume seeds have been characterized structurally. The presence of Cys-Cys in single or double chains shows a new pattern of proteins structurally not so closely related to STI. Therefore, briefly, with regard to cysteine content, plant Kunitz proteinase inhibitors may be classified into four groups: no Cys-Cys at all, one, two and more than two Cys residues. Functional properties and diversity of these proteins are also briefly discussed.
Oliva
Maria Luiza V
ML
Department of Biochemistry, Universidade Federal de São Paulo-Escola Paulista de Medicina, São Paulo, Brazil. olivaml.bioq@epm.br
Silva
Mariana C C
MC
Sallai
Roberto C
RC
Brito
Marlon V
MV
Sampaio
Misako U
MU
D000595:Amino Acid Sequence; D003545:Cysteine; D007887:Fabaceae; D006801:Humans; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000145:classification* / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry / Q000145:classification* / Q000378:metabolism; D011487:Protein Conformation; D012639:Seeds
C053865:Kunitz-type protease inhibitor, plant; D010455:Peptides; D010940:Plant Proteins; D010447:Peptide Hydrolases; D003545:Cysteine