Functional analysis of the cucumisin propeptide as a potent inhibitor of its mature enzyme

Journal of Biological Chemistry

Volumn 285, Issue 39, 2010, Pages 29797-29807

  Nakagawa, Masataka ^a   Ueyama, Megumi ^a   Tsuruta, Hiroki ^a   Uno, Tomohide ^a   Kanamaru, Kengo ^a   Mikami, Bunzo ^b   Yamagata, Hiroshi ^a  

^a KOBE UNIVERSITY   (Japan)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; ENZYMES; ESCHERICHIA COLI; HYDROPHOBICITY; PHOSPHATASES;

A PLANTS; ARABIDOPSIS; COGNATE PROTEASE; CUCUMIS MELO; DELETION ANALYSIS; HYDROPHOBIC CLUSTERS; HYDROPHOBIC REGIONS; INHIBITORY ACTIVITY; POTENT INHIBITOR; PROPEPTIDES; SECONDARY STRUCTURES; SERINE PROTEASE; SIGNAL PEPTIDE; SITE DIRECTED MUTAGENESIS; STRUCTURAL INFORMATION; SUBTILISIN; THERMAL UNFOLDING; TRIPEPTIDE;

GENE ENCODING;

ARABIDOPSIS PROTEIN; ASPARAGINE; COMPLEMENTARY DNA; CUCUMISIN; ENZYME INHIBITOR; GLYCINE; LEUCINE; METHIONINE; PROTEIN ARA12; PROTEIN PRECURSOR; PROTEIN RSP1; SUBTILISIN; TRIPEPTIDE; UNCLASSIFIED DRUG; VALINE; ARA12 PROTEIN, ARABIDOPSIS; ENZYME PRECURSOR; RECOMBINANT PROTEIN; SERINE PROTEINASE;

ARABIDOPSIS; ARTICLE; CIRCULAR DICHROISM; COMPETITIVE INHIBITION; CONTROLLED STUDY; HYDROPHOBICITY; MELON; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; CHEMISTRY; CUCURBITACEAE; ENZYME ACTIVATION; ENZYMOLOGY; GENETICS; METABOLISM; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; RICE;

ARABIDOPSIS; BACTERIA (MICROORGANISMS); CUCUMIS; CUCUMIS MELO; ESCHERICHIA COLI;

ARABIDOPSIS; ARABIDOPSIS PROTEINS; CUCURBITACEAE; ENZYME ACTIVATION; ENZYME PRECURSORS; MUTAGENESIS, SITE-DIRECTED; ORYZA SATIVA; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES; SUBTILISINS;

EID: 77956932515     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.083162     Document Type: Article

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