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The characterization of 5 histidine-serine mutants of human 5-lipoxygenase

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
186
Issue
3
Identifiers
DOI: 10.1016/s0006-291x(05)81542-6
Disciplines
  • Biology

Abstract

The physical and catalytic properties of 5 histidine-serine mutants of human 5-lipoxygenase (5-LO) have been characterized. The mutants HS363, HS391 and HS400 have activities, pH optima and stabilities similar to those of the wild type enzyme. The iron content of each of these mutants is 0.30 – 0.53 mol Fe/mol 5-LO which is within the range observed for the wild type enzyme. HS368 contains iron (0.15 and 0.43 mol Fe/mol 5-LO in 2 preparations) but has no detectable oxygenase, leukotriene A4 synthase or anaerobic arachidonate-dependent hydroperoxidase activities. HS368 does have significant reducing agent-dependent hydroperoxidase activity suggesting that His-368 may not be an iron ligand but rather may be involved in interactions with arachidonic acid or the formation of the arachidonyl radical intermediate. HS373 contains no iron and has no detectable activities.

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