Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway

Journal of Biological Chemistry

Volumn 274, Issue 17, 1999, Pages 11582-11586

  Qian, Yimei ^a   Varlamov, Oleg ^a   Fricker, Lloyd D ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE H; CARBOXYPEPTIDASE; GLUTAMIC ACID;

AMINO ACID COMPOSITION; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME REGULATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; NONHUMAN; PANCREAS ISLET BETA CELL; PRIORITY JOURNAL; RAT; AMINO ACID SEQUENCE; ANIMAL; ARMYWORM; CELL LINE; CHEMISTRY; CYTOLOGY; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; MOUSE; PANCREAS ISLET; PROTEIN BINDING; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; CARBOXYPEPTIDASE H; CARBOXYPEPTIDASES; CELL LINE; GLUTAMIC ACID; ISLETS OF LANGERHANS; MICE; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; RATS; SEQUENCE HOMOLOGY, AMINO ACID; SPODOPTERA; SUBSTRATE SPECIFICITY;

EID: 0033596982     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.17.11582     Document Type: Article

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