| pubmed-article:7947938 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7947938 | lifeskim:mentions | umls-concept:C0010749 | lld:lifeskim |
| pubmed-article:7947938 | lifeskim:mentions | umls-concept:C0010798 | lld:lifeskim |
| pubmed-article:7947938 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:7947938 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:7947938 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7947938 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:7947938 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:7947938 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:7947938 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:7947938 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7947938 | pubmed:dateCreated | 1994-12-22 | lld:pubmed |
| pubmed-article:7947938 | pubmed:abstractText | Cytochrome P-450BM-3 from Bacillus megaterium is a soluble, catalytically self-sufficient fatty acid mono-oxygenase that resembles the Class II P-450 systems of the eukaryotic endoplasmic reticulum. Its single polypeptide chain contains both a P-450 heme domain and an NADPH:P-450 reductase domain, each of which bears significant structural and functional homology with its microsomal counterparts. We report here that cytochrome c, which can accept NADPH-derived electrons from the reductase domain of P-450-BM-3, did not inhibit myristate hydroxylation catalyzed by P-450BM-3 or by two reductase domain mutant enzymes (W574Y, W574F) which have diminished hydroxylase activity relative to wild-type enzyme but retain cytochrome c reductase activity levels comparable to wild-type enzyme. Because reduced cytochrome c generated independently of the reductase domain of P-450BM-3 did not support myristate hydroxylation, it seems likely that cytochrome c binds to a site on the reductase domain which does not overlap the site of the heme domain interaction. We also found that myristate did not inhibit P-450BM-3-mediated cytochrome c reduction. Since neither substrate inhibited the conversion of the other, we conclude that the rate-limiting steps for both myristate hydroxylation and cytochrome c reduction by P-450BM-3 do not involve electron transfer through the reductase domain. | lld:pubmed |
| pubmed-article:7947938 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7947938 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7947938 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7947938 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7947938 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7947938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7947938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7947938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7947938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7947938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7947938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7947938 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7947938 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7947938 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:7947938 | pubmed:author | pubmed-author:FulcoA JAJ | lld:pubmed |
| pubmed-article:7947938 | pubmed:author | pubmed-author:KleinM LML | lld:pubmed |
| pubmed-article:7947938 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7947938 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:7947938 | pubmed:volume | 1201 | lld:pubmed |
| pubmed-article:7947938 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7947938 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7947938 | pubmed:pagination | 245-50 | lld:pubmed |
| pubmed-article:7947938 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7947938 | pubmed:meshHeading | pubmed-meshheading:7947938-... | lld:pubmed |
| pubmed-article:7947938 | pubmed:meshHeading | pubmed-meshheading:7947938-... | lld:pubmed |
| pubmed-article:7947938 | pubmed:meshHeading | pubmed-meshheading:7947938-... | lld:pubmed |
| pubmed-article:7947938 | pubmed:meshHeading | pubmed-meshheading:7947938-... | lld:pubmed |
| pubmed-article:7947938 | pubmed:meshHeading | pubmed-meshheading:7947938-... | lld:pubmed |
| pubmed-article:7947938 | pubmed:meshHeading | pubmed-meshheading:7947938-... | lld:pubmed |
| pubmed-article:7947938 | pubmed:meshHeading | pubmed-meshheading:7947938-... | lld:pubmed |
| pubmed-article:7947938 | pubmed:meshHeading | pubmed-meshheading:7947938-... | lld:pubmed |
| pubmed-article:7947938 | pubmed:meshHeading | pubmed-meshheading:7947938-... | lld:pubmed |
| pubmed-article:7947938 | pubmed:meshHeading | pubmed-meshheading:7947938-... | lld:pubmed |
| pubmed-article:7947938 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7947938 | pubmed:articleTitle | The interaction of cytochrome c and the heme domain of cytochrome P-450BM-3 with the reductase domain of cytochrome P-450BM-3. | lld:pubmed |
| pubmed-article:7947938 | pubmed:affiliation | Department of Biological Chemistry, UCLA School of Medicine. | lld:pubmed |
| pubmed-article:7947938 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7947938 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7947938 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
