The tetra-aspartate motif in the activation peptide of human cationic trypsinogen is essential for autoactivation control but not for enteropeptidase recognition

Journal of Biological Chemistry

Volumn 280, Issue 33, 2005, Pages 29645-29652

  Nemoda, Zsófia ^a   Sahin Tóth, Miklós ^a,b  

^a BOSTON UNIVERSITY   (United States)

^b Evans 433 ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CHEMICAL BONDS; COMPUTER SIMULATION; HYDROPHOBICITY; MUTAGENESIS;

ACTIVATION PEPTIDES; ENTEROPEPTIDASE; HUMAN CATIONIC TRYPSINOGENS; SCISSILE BOND;

POLYPEPTIDES;

ALANINE; ASPARAGINE; ASPARTIC ACID; ENTEROPEPTIDASE; ISOLEUCINE; LYSINE; PEPTIDE; TRYPSINOGEN;

ACIDITY; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL BOND; ENZYME ACTIVATION; ENZYME MECHANISM; ENZYME REPRESSION; ENZYME SPECIFICITY; GENE MUTATION; GENETIC CONSERVATION; HUMAN; HYDROPHOBICITY; MOLECULAR MODEL; MOLECULAR RECOGNITION; MUTANT; NONHUMAN; PANCREAS; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; VERTEBRATE;

AMINO ACID MOTIFS; ANIMALS; ASPARTIC ACID; CATTLE; CONSERVED SEQUENCE; ENTEROPEPTIDASE; ENZYME ACTIVATION; ENZYME PRECURSORS; HUMANS; TRYPSIN; TRYPSINOGEN;

BOVINAE; VERTEBRATA;

EID: 23844507473     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M505661200     Document Type: Article

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