Conversion of human 15-lipoxygenase to an efficient 12-lipoxygenase: The side-chain geometry of amino acids 417 and 418 determine positional specificity

Protein Engineering, Design and Selection

Volumn 8, Issue 3, 1995, Pages 275-282

  Sloane, David L ^a   Leung, Regina ^a   Barnett, Jim ^a   Craik, Charles S ^b   Sigal, Elliott ^a  

^a ROCHE BIOSCIENCE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Arachidonic acid; Conserved differences; Lipoxygenase; Regiospecificity; Substrate specificity

Indexed keywords

ARACHIDONATE 12 LIPOXYGENASE; ARACHIDONATE 15 LIPOXYGENASE; ARACHIDONIC ACID; ENZYME VARIANT; LINOLEIC ACID;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BACULOVIRUS; CONTROLLED STUDY; DNA TRANSFECTION; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; HUMAN; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ARACHIDONATE 12-LIPOXYGENASE; ARACHIDONATE 15-LIPOXYGENASE; ARACHIDONIC ACID; BACULOVIRIDAE; BASE SEQUENCE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; COMPARATIVE STUDY; ESCHERICHIA COLI; HUMAN; KINETICS; LINOLEIC ACID; LINOLEIC ACIDS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0029042095     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/8.3.275     Document Type: Article

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