Catalytic properties of two human leukotriene B4 ω-hydroxylase P450s

Autor:	Yasushi Kikuta, Emi Kusunose, Masamichi Kusunose
Rok vydání:	2002
Předmět:	chemistry.chemical_classification Leukotriene B4 Structural similarity CYP4F3 Protein primary structure General Medicine Biology law.invention chemistry.chemical_compound Exon Enzyme Biochemistry chemistry law Recombinant DNA lipids (amino acids peptides and proteins) Arachidonic acid
Zdroj:	International Congress Series. 1233:139-142
ISSN:	0531-5131
DOI:	10.1016/s0531-5131(02)00289-3
Popis:	We have investigated the catalytic properties of recombinant proteins of two human leukotriene B4 (LTB4) ω-hydroxylases (CYP4F2 and CYP4F3) as well as the gene structures of these closely related enzymes. When expressed in yeast cells and purified to homogeneity, both enzymes metabolized not only LTB4, but also other lipoxygenase-dependent arachidonic acid metabolites such as 12-HETE. However, there were some striking differences between CYP4F2 and CYP4F3: (1) the Km of CYP4F2 for LTB4 (60 μM) was 94-fold higher than that of CYP4F3 (0.64 μM); (2) CYP4F3 preferentially ω-hydroxylated lipoxin B4 over lipoxin A4, whereas CYP4F2 was only capable of metabolizing lipoxin A4; (3) in contrast to CYP4F3, CYP4F2 was very unstable for storage. The CYP4F2 and CYP4F3 genes displayed a marked structural similarity. However, the structure of exon III was quite different. Variation in exon III resulted in a low homologous region (27%) within the primary structure of the enzymes.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::e7cebbafa41d4ca8f49982a8a2761de8 https://doi.org/10.1016/s0531-5131(02)00289-3 Zobrazit plný text záznamu Full Text from ScienceDirect