Literature DB >> 7825866

On the positional specificity of 15-lipoxygenase.

D L Sloane1, E Sigal.   

Abstract

The lipoxygenases comprise a family of fatty acid dioxygenases that are involved in a variety of inflammatory conditions. Various approaches have been taken in order to understand the different regiospecificities of the different lipoxygenases. Here we have reviewed the current knowledge of the structural features of the substrate and of the enzyme that form the basis of the regiospecificity of 15-lipoxygenase. Earlier experiments on the structural features of the substrate were reviewed, as well as more recent results of site-directed mutagenesis studies. The structure of the soybean lipoxygenase isoform-1 was also briefly reviewed.

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Year:  1994        PMID: 7825866     DOI: 10.1111/j.1749-6632.1994.tb52727.x

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN: 0077-8923            Impact factor:   5.691


  3 in total

1.  Relation between positional specificity and chirality in mammalian lipoxygenases.

Authors:  S T Prigge; B J Gaffney; L M Amzel
Journal:  Nat Struct Biol       Date:  1998-03

2.  Substrate specificity changes for human reticulocyte and epithelial 15-lipoxygenases reveal allosteric product regulation.

Authors:  Aaron T Wecksler; Victor Kenyon; Joshua D Deschamps; Theodore R Holman
Journal:  Biochemistry       Date:  2008-06-21       Impact factor: 3.162

3.  Lipoxygenase Activity Accelerates Programmed Spore Germination in Aspergillus fumigatus.

Authors:  Gregory J Fischer; William Bacon; Jun Yang; Jonathan M Palmer; Taylor Dagenais; Bruce D Hammock; Nancy P Keller
Journal:  Front Microbiol       Date:  2017-05-09       Impact factor: 5.640

  3 in total

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