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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1994-11-29
|
| pubmed:databankReference | |
| pubmed:abstractText |
Cytochrome P460 and hydroxyamine oxidoreductase of Nitrosomonas europaea both catalyze the oxidation of hydroxylamine and contain a 460 nm-absorbing chromophore. The gene (cyp) encoding cytochrome P460 was cloned and sequenced. The predicted amino acid sequence contains a single c-heme binding motif (CXXCH) near the carboxy-terminus. Cytochrome P460 shows little sequence homology to other c-cytochromes including hydroxyamine oxidoreductase. The presence of a signal peptide and a possible c-heme binding site suggest that the cytochrome P460 of N. europaea is periplasmic.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0014-5793
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
|
| pubmed:volume |
353
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
324-6
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7957885-Amino Acid Sequence,
pubmed-meshheading:7957885-Base Sequence,
pubmed-meshheading:7957885-Binding Sites,
pubmed-meshheading:7957885-Cloning, Molecular,
pubmed-meshheading:7957885-Cytochromes,
pubmed-meshheading:7957885-Genes, Bacterial,
pubmed-meshheading:7957885-Heme,
pubmed-meshheading:7957885-Molecular Sequence Data,
pubmed-meshheading:7957885-Nitrosomonas,
pubmed-meshheading:7957885-Sequence Analysis, DNA
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
The primary structure of cytochrome P460 of Nitrosomonas europaea: presence of a c-heme binding motif.
|
| pubmed:affiliation |
Graduate Program in Biochemistry, University of Minnesota, St. Paul 55108.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|