Sequence determinants for the positional specificity of mammalian and plant lipoxygenases

Advances in Experimental Medicine and Biology

Volumn 469, Issue , 2000, Pages 91-97

  Borngraber S ^a   Kuban, R J ^a   Kuhn H ^a  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

LIPOXYGENASE;

CATALYSIS; CHEMICAL MUTAGENESIS; CONFERENCE PAPER; ENZYME SPECIFICITY; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

MAMMALIA;

EID: 0034465429     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper

References (15)

1. Simultaneous expression of leukocyte-type 12-lipoxygenase and reticulocyte-type 15-lipoxygenase in rabbits
2. The three-dimensional structure of an arachidonic acid 15-lipoxygenase
3. Phenylalanine 353 is a primary determinant for the positional specificity of mammalian 15-lipoxygenases
4. Structure-function properties of human platelet 12-lipoxygenase: Chimeric enzyme and in vitro mutagenesis studies
5. The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity
6. Arachidonate 12-lipoxygenase of rat pineal glands: Catalytic properties and primary structure deduced from its cDNA
7. The stereochemistry of the reaction of lipoxygenases and their metabolites. A proposed nomenclature for lipoxygenases and related enzymes
8. Bacterial expression, purification and partial characterization of recombinant rabbit reticulocyte 15-lipoxygenase
9. Regio-and stereoselectivity of the dioxygenation reaction catalyzed by (S)-type lipoxygenases or by the cyclooxygenase activity of prostaglandin H synthase
10. Crystal structure of soybean lipoxygenase L-1 at 1.4 Å resolution
11. Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme
12. A primary determinant for lipoxygenase positional specificity
13. Conversion of human 15-lipoxygenase to an efficient 12-lipoxygenase: The side-chain geometry of amino acids 417 and 418 determines positional specificity
14. Site-directed mutagenesis studies on the iron binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase
15. Rat 12-lipoxygenase: Mutations of amino acids implicated in the positional specificity of 15- and 12-lipoxygenases