Structure-to-function relationship of mini-lipoxygenase, a 60-kDa fragment of soybean lipoxygenase-1 with lower stability but higher enzymatic activity

Journal of Biological Chemistry

Volumn 278, Issue 20, 2003, Pages 18281-18288

  Di Venere, Almerinda ^a,b   Salucci, Maria Luisa ^c   Van Zadelhoff, Guus ^d   Veldink, Gerrit ^d   Mei, Giampiero ^a,b   Rosato, Nicola ^a,b,e   Finazzi Agrò, Alessandro ^b   Maccarrone, Mauro ^f  

^a INFM   (Italy)

^b UNIVERSITY OF ROME TOR VERGATA   (Italy)

^c UNIVERSITY OF L'AQUILA   (Italy)

^d UTRECHT UNIVERSITY   (Netherlands)

^e SAN GIOVANNI CALIBITA FATEBENEFRATELLI HOSPITAL   (Italy)

^f UNIVERSITY OF TERAMO   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; DIGESTIVE SYSTEM; FATTY ACIDS; FLUORESCENCE; HYDRATION; METABOLISM; SPECTROSCOPIC ANALYSIS;

CIRCULAR DICHROISM SPECTROSCOPY;

ENZYMES;

8 ANILINO 1 NAPHTHALENESULFONIC ACID; GUANIDINE; ICOSATETRAENOIC ACID; LINOLEIC ACID; LIPOXYGENASE; LIPOXYGENASE I; UNCLASSIFIED DRUG; 1-ANILINO-8-NAPHTHALENESULFONATE; ARACHIDONIC ACID DERIVATIVE; LIPOXYGENASE L 1; LIPOXYGENASE L-1;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SOYBEAN; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; KINETICS; METABOLISM; PROTEIN BINDING; PROTEIN CONFORMATION; RABBIT; SPECTROFLUOROMETRY; STRUCTURE ACTIVITY RELATION; TIME;

EUKARYOTA; GLYCINE MAX;

ANILINO NAPHTHALENESULFONATES; ANIMALS; ARACHIDONIC ACIDS; BINDING SITES; CIRCULAR DICHROISM; DOSE-RESPONSE RELATIONSHIP, DRUG; GUANIDINE; KINETICS; LIPOXYGENASE; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; RABBITS; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP; TIME FACTORS;

EID: 0038381477     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M212122200     Document Type: Article

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