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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-3-14
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pubmed:abstractText |
Fatty acid hydroperoxide lyase (HPO lyase) is an enzyme that cleaves hydroperoxides of polyunsaturated fatty acids to form short chain aldehydes and omega-oxoacids. Spectrophotometric analyses of HPO lyase highly purified from green bell pepper fruits indicate that it is a heme protein. The heme species was revealed to be heme b (protoheme IX) from the absorption spectrum of the pyridine hemochromogen. Although the spectrum highly resembles that of a plant cytochrome P450, allene oxide synthase from flaxseed, CO treatment of the enzyme caused no appearance of a peak at 450 nm, which is an essential diagnostic feature of a cytochrome P450. Internal amino acid sequences determined with peptide fragments obtained from the lyase showed no homology with any reported sequences.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-291X
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
207
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
438-43
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
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pubmed:year |
1995
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pubmed:articleTitle |
Fatty acid hydroperoxide lyase is a heme protein.
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pubmed:affiliation |
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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