The PA domain is crucial for determining optimum substrate length for soybean protease C1: Structure and kinetics correlate with molecular function

Plant Physiology and Biochemistry

Volumn 53, Issue , 2012, Pages 27-32

  Tan Wilson, Anna ^a   Bandak, Basel ^b   Prabu Jeyabalan, Moses ^b,c  

^a BINGHAMTON UNIVERSITY   (United States)

^b UNIVERSITY OF SCRANTON   (United States)

^c Geisinger Health Geisinger Commonwealth School of Medicine   (United States)

Author keywords

Active site; Homology modeling; PA domain; Proteolytic enzyme; Storage protein mobilization; Substrate binding; Subtilisin

Indexed keywords

AMINO ACID; BETA CONGLYCININ PROTEIN, GLYCINE MAX; BETA-CONGLYCININ PROTEIN, GLYCINE MAX; GLOBULIN; PLANT ANTIGEN; PROTEASE C1; PROTEINASE; SEED STORAGE PROTEIN; SOYBEAN PROTEIN; SUBTILASE, PLANT; SUBTILISIN; VEGETABLE PROTEIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; KINETICS; METABOLISM; PROTEIN TERTIARY STRUCTURE; SOYBEAN; TOMATO;

AMINO ACIDS; ANTIGENS, PLANT; ENDOPEPTIDASES; GLOBULINS; KINETICS; LYCOPERSICON ESCULENTUM; MODELS, MOLECULAR; PLANT PROTEINS; PROTEIN STRUCTURE, TERTIARY; SEED STORAGE PROTEINS; SOYBEAN PROTEINS; SOYBEANS; SUBSTRATE SPECIFICITY; SUBTILISINS;

GLYCINE MAX; LYCOPERSICON ESCULENTUM;

EID: 84856112751     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2012.01.005     Document Type: Article

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