Primary structure of aspergillopepsin I deduced from nucleotide sequence of the gene and aspartic acid-76 is an essential active site of the enzyme for trypsinogen activation

Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular

Volumn 1204, Issue 2, 1994, Pages 257-264

  Shintani, Takahiro ^a   Ichishima, Eiji ^a  

^a Laboratory of Molecular Enzymology Department of Applied Biological Chemistry Faculty of Agriculture ^*  (Japan)

Author keywords

(Aspergillus); Aspartic proteinase; Aspergillopepsin I; Specificity; Trypsinogen activation

Indexed keywords

ASPARTIC PROTEINASE; ASPERGILLOPEPSIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; ASPERGILLUS; DNA SEQUENCE; ENZYME SPECIFICITY; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ASPARTIC ACID; ASPARTIC ENDOPEPTIDASES; ASPERGILLUS; BASE SEQUENCE; BINDING SITES; COMPARATIVE STUDY; GENES, FUNGAL; HUMAN; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPSIN A; SERINE; SUBSTRATE SPECIFICITY; TRYPSINOGEN;

ASPERGILLUS;

EID: 0028269367     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/0167-4838(94)90016-7     Document Type: Article

References (40)

1. PCR Protocols