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PMID: 2829172 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Molecular cloning and amino acid sequence of human 5-lipoxygenase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 85 ·No. 1 ·1988-01-00 ·Pages 26-30

Matsumoto T, Funk CD, Rådmark O, Höög JO, Jörnvall H, Samuelsson B

Abstract

5-Lipoxygenase (EC 1.13.11.34), a Ca2+-and ATP-requiring enzyme, catalyzes the first two steps in the biosynthesis of the peptidoleukotrienes and the chemotactic factor leukotriene B4. A cDNA clone corresponding to 5-lipoxygenase was isolated from a human lung lambda gt11 expression library by immunoscreening with a polyclonal antibody. Additional clones from a human placenta lambda gt11 cDNA library were obtained by plaque hybridization with the 32P-labeled lung cDNA clone. Sequence data obtained from several overlapping clones indicate that the composite cDNAs contain the complete coding region for the enzyme. From the deduced primary structure, 5-lipoxygenase encodes a 673 amino acid protein with a calculated molecular weight of 77,839. Direct analysis of the native protein and its proteolytic fragments confirmed the deduced composition, the amino-terminal amino acid sequence, and the structure of many internal segments. 5-Lipoxygenase has no apparent sequence homology with leukotriene A4 hydrolase or Ca2+ -binding proteins. RNA blot analysis indicated substantial amounts of an mRNA species of approximately equal to 2700 nucleotides in leukocytes, lung, and placenta.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Arachidonate 5-Lipoxygenase/genetics Arachidonate Lipoxygenases/genetics Base Sequence Cloning, Molecular DNA/genetics DNA Restriction Enzymes Female Genes Humans Lung/enzymology Molecular Sequence Data Nucleotide Mapping Placenta/enzymology RNA, Messenger/genetics
Chemicals
Amino Acids RNA, Messenger DNA Arachidonate Lipoxygenases Arachidonate 5-Lipoxygenase DNA Restriction Enzymes
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Matsumoto T
Department of Physiological Chemistry, Karolinska Institutet, Stockholm, Sweden.
Funk C D
Rådmark O
Höög J O
Jörnvall H
Samuelsson B
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.85.1.26
Published
1988-01-00
Pages
26-30
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC279474
Subset
IM
Databases
GENBANK
J03571
Corrections
ErratumIn
-
External Links
PubMed source DOI: 10.1073/pnas.85.1.26 PMC Full Text View journal details
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