Membrane type-1 matrix metalloproteinase functions as a proprotein self-convertase: Expression of the latent zymogen in Pichia pastoris, autolytic activation, and the peptide sequence of the cleavage forms

Journal of Biological Chemistry

Volumn 278, Issue 10, 2003, Pages 8257-8260

  Rozanov, Dmitri V ^b   Strongin, Alex Y ^a  

^a BURNHAM INSTITUTE   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CHEMICAL ACTIVATION; LIQUID CHROMATOGRAPHY; SURFACE PROPERTIES; TUMORS;

PROTEOLYTIC PATHWAYS;

ENZYMES;

ENZYME PRECURSOR; FURIN; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE; METALLOPROTEINASE; SERINE PROTEINASE; SUBTILISIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELL COMPARTMENTALIZATION; CELL MIGRATION; ENZYME ACTIVITY; ENZYME METABOLISM; FAST PROTEIN LIQUID CHROMATOGRAPHY; MITOCHONDRIAL MEMBRANE; NONHUMAN; NUCLEOTIDE SEQUENCE; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN DOMAIN; CHEMISTRY; ENZYME ACTIVATION; GENETICS; HYDROLYSIS; METABOLISM; PICHIA;

PICHIA PASTORIS;

AMINO ACID SEQUENCE; ENZYME ACTIVATION; HYDROLYSIS; MATRIX METALLOPROTEINASES, MEMBRANE-ASSOCIATED; METALLOENDOPEPTIDASES; PICHIA; PROPROTEIN CONVERTASES; SUBTILISINS;

EID: 0037424402     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M213246200     Document Type: Article

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