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Human CYP4Z1 catalyzes the in-chain hydroxylation of lauric acid and myristic acid
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Andy Zöllner
, Calin-Aurel Dragan , Dominik Pistorius , Rolf Müller , Helge B. Bode , Frank T. Peters , Hans H. Maurer and Matthias Bureik
Published/Copyright:
December 17, 2008
Abstract
Overexpression of human CYP4Z1, a cytochrome P450 enzyme, has been correlated with poor prognosis in human cancer. However, its catalytic properties are not yet known. We expressed this P450 in Schizosaccharomyces pombe and demonstrate by whole-cell biotransformation assays CYP4Z1-dependent in-chain hydroxylation of lauric and myristic acid, which in both cases leads to the formation of four different monohydroxylated products at positions ω-2, ω-3, ω-4, and ω-5, respectively. The CYP4Z1-expressing fission yeast should be a new valuable tool for testing cancer drugs or for the development of new prodrug strategies.
Keywords: breast cancer; cancer treatment; cytochrome P450; fatty acid hydroxylation; Schizosaccharomyces pombe; whole-cell biotransformation
Received: 2008-11-21
Accepted: 2008-12-3
Published Online: 2008-12-17
Published in Print: 2009-04-01
©2009 by Walter de Gruyter Berlin New York
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Keywords for this article
breast cancer;
cancer treatment;
cytochrome P450;
fatty acid hydroxylation;
Schizosaccharomyces pombe;
whole-cell biotransformation
Articles in the same Issue
- Minireview
- Central nervous system: cholesterol turnover, brain development and neurodegeneration
- Protein Structure and Function
- Structure-function relationship of the human antimicrobial peptide LL-37 and LL-37 fragments in the modulation of TLR responses
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- Flavivirus NS5 associates with host-cell proteins zonula occludens-1 (ZO-1) and regulating synaptic membrane exocytosis-2 (RIMS2) via an internal PDZ binding mechanism
- Membranes, Lipids, Glycobiology
- Co-expression of 9-O-acetylated sialoglycoproteins and their binding proteins on lymphoblasts of childhood acute lymphoblastic leukemia: an anti-apoptotic role
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- Proteolysis
- Staphylococcal cysteine protease staphopain B (SspB) induces rapid engulfment of human neutrophils and monocytes by macrophages
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