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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
31
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pubmed:dateCreated |
1993-11-29
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pubmed:databankReference | |
pubmed:abstractText |
An expression vector for NADH-cytochrome b5 reductase containing a thrombin cleavage site directly before the N-terminal glycine residue of the flavoprotein was used to isolate the non-myristoylated enzyme by thrombin cleavage of the initial fusion protein of a short segment of the multiple cloning site of the plasmid vector and the reductase. This flavoprotein preparation, containing only the 28-residue N-terminal peptide segment of the membrane-binding domain of the mammalian enzyme, binds to phospholipid vesicles and interacts with membrane-bound cytochrome b5. The effect of N-myristoylation of the enzyme therefore appears to be limited to facilitating and stabilizing interactions with phospholipid vesicles. However, the relatively short intervening peptide sequence that separates the crucial peptide membrane-binding domain from lysine 41, which has been implicated in the active-site interaction with cytochrome b5 (Strittmatter, P., Kittler, J. M., Coghill, J. E., and Ozols, J. (1992) J. Biol. Chem. 267, 2519-2523), provides some limitation of the distance from the membrane surface for the interactions required for rapid electron transfer from the flavin of the reductase to the heme of cytochrome b5.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome-B(5) Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes b5,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Dimyristoylphosphatidylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Myristates,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23168-71
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8226835-Base Sequence,
pubmed-meshheading:8226835-Cytochrome Reductases,
pubmed-meshheading:8226835-Cytochrome-B(5) Reductase,
pubmed-meshheading:8226835-Cytochromes b5,
pubmed-meshheading:8226835-DNA Primers,
pubmed-meshheading:8226835-Dimyristoylphosphatidylcholine,
pubmed-meshheading:8226835-Membrane Lipids,
pubmed-meshheading:8226835-Molecular Sequence Data,
pubmed-meshheading:8226835-Myristates,
pubmed-meshheading:8226835-Oxidation-Reduction,
pubmed-meshheading:8226835-Recombinant Fusion Proteins,
pubmed-meshheading:8226835-Structure-Activity Relationship
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pubmed:year |
1993
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pubmed:articleTitle |
Interaction of non-myristoylated NADH-cytochrome b5 reductase with cytochrome b5-dimyristoylphosphatidylcholine vesicles.
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pubmed:affiliation |
Department of Biochemistry, University of Connecticut Health Center, Farmington 06030-3305.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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