Human platelet 12-lipoxygenase: Naturally occurring Q261/R261 variants and N544L mutant show altered activity but unaffectedsubstrate binding and membrane association behavior

International Journal of Molecular Medicine

Volumn 24, Issue 6, 2009, Pages 759-764

  Aleem, Ansari M ^a,e   Wells, Leigh ^a,f   Jankun, Jerzy ^a,b   Walther, Matthias ^c   Kuhn, Hartmut ^c   Reinartz, Jeannette ^d   Skrzypczak Jankun, Ewa ^a  

^a MEDICAL COLLEGE OF OHIO   (United States)

^b MEDICAL UNIVERSITY OF GDANSK   (Poland)

^c CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^d American Diagnostica GmbH   (Germany)

^e KING SAUD UNIVERSITY   (Saudi Arabia)

^f Des Moines University College of Osteopathic Medicine   (United States)

Author keywords

12 Lipoxygenase; Arachidonic acid binding; Membrane binding; Single nucleotide polymorphism; SNP R261Q

Indexed keywords

ALANINE; ARACHIDONATE 12 LIPOXYGENASE; ARGININE; ASPARAGINE; GLUTAMINE; HISTIDINE; ISOLEUCINE; LEUCINE; MUTANT PROTEIN; OLIGOMER;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME DEGRADATION; ENZYME MODIFICATION; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; HUMAN; HUMAN CELL; MEMBRANE BINDING; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN VARIANT; SIGNAL TRANSDUCTION; SINGLE NUCLEOTIDE POLYMORPHISM; THROMBOCYTE; WILD TYPE;

ALLOSTERIC SITE; ARACHIDONATE 12-LIPOXYGENASE; BLOOD PLATELETS; CELL MEMBRANE; ENZYME STABILITY; HUMANS; MODELS, MOLECULAR; POLYMORPHISM, SINGLE NUCLEOTIDE; PROTEIN BINDING; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 70350772548     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm_00000289     Document Type: Article

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