Publication Date:
1997-09-26
Description:
A distant relative of catalase that is specialized for metabolism of a fatty acid hydroperoxide was identified. This heme peroxidase occurs in coral as part of a fusion protein, the other component of which is a lipoxygenase that forms the hydroperoxide substrate. The end product is an unstable epoxide (an allene oxide) that is a potential precursor of prostaglandin-like molecules. These results extend the known chemistry of catalase-like proteins and reveal a distinct type of enzymatic construct involved in the metabolism of polyunsaturated fatty acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koljak, R -- Boutaud, O -- Shieh, B H -- Samel, N -- Brash, A R -- GM49502/GM/NIGMS NIH HHS/ -- TW00404/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 26;277(5334):1994-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232-6602, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9302294" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Arachidonic Acid/metabolism
;
Binding Sites
;
Catalase/chemistry
;
Catalysis
;
Cloning, Molecular
;
Cnidaria/*enzymology/genetics
;
Hydrogen Peroxide/metabolism
;
*Intramolecular Oxidoreductases
;
Isomerases/chemistry
;
Lipoxygenase/*chemistry/genetics/isolation & purification/metabolism
;
Molecular Sequence Data
;
Peroxidase/*chemistry/genetics/isolation & purification/metabolism
;
Peroxidases/*chemistry/isolation & purification/metabolism
;
Recombinant Proteins/metabolism
;
Sequence Homology, Amino Acid
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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