Characterization of recombinant CDR1, an Arabidopsis aspartic proteinase involved in disease resistance

Journal of Biological Chemistry

Volumn 282, Issue 43, 2007, Pages 31358-31365

  Simões, Isaura ^a   Faro, Rosário ^a   Bur, Daniel ^b   Faro, Carlos ^a  

^a UNIVERSITY OF COIMBRA   (Portugal)

^b ACTELION PHARMACEUTICALS LTD   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS THALIANA; CONSTITUTIVE DISEASE RESISTANCE 1 (CDR1); ENZYMATIC PROPERTIES;

BIOCHEMISTRY; DISEASES; GENES; PH EFFECTS; PLANTS (BOTANY);

ENZYME KINETICS;

4 (2 AMINOETHYL)BENZENESULFONYL FLUORIDE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMASTATIN; ASPARTIC PROTEINASE; CALCIUM; CONSTITUTIVE DISEASE RESISTANCE 1; DITHIOTHREITOL; EDETIC ACID; GLUTATHIONE; GLUTATHIONE DISULFIDE; MAGNESIUM; MANGANESE; MUTANT PROTEIN; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; PEPSTATIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG; ZINC;

ARABIDOPSIS; ARTICLE; CATALYSIS; CONTROLLED STUDY; DRUG MECHANISM; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ARABIDOPSIS; ARABIDOPSIS PROTEINS; ASPARTIC ENDOPEPTIDASES; BINDING SITES; CLONING, MOLECULAR; CONSENSUS SEQUENCE; DIMERIZATION; DNA, COMPLEMENTARY; DNA, PLANT; ESCHERICHIA COLI; FLUORESCEIN-5-ISOTHIOCYANATE; FLUORESCENT DYES; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEIC ACID AMPLIFICATION TECHNIQUES; PLANT DISEASES; PROTEIN BINDING; PROTEIN SORTING SIGNALS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TEMPERATURE;

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 35748950440     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M702477200     Document Type: Article

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