Linked Life Data

3947063

Source:http://linkedlifedata.com/resource/pubmed/id/3947063

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-3-12
pubmed:abstractText
The complete amino acid sequence of rat liver microsomal cytochrome P-450d (induced by isosafrole) was deduced by microsequence analysis of the tryptic peptides after separation by reverse-phase HPLC and alignment by comparison to the cDNA sequence reported by K. Kawajiri, O. Gotoh, K. Sogawa, Y. Tagashira, M. Muramatsu, and Y. Fujii-Kuriyama (1984, Proc. Natl. Acad. Sci. USA 81, 1649-1653). Results from the two approaches are in complete agreement with the exception of two residues, Lys-30 (Arg in cDNA) and Phe-261 (Ser in cDNA). As previously reported by us (L. H. Botelho, D. E. Ryan, P.-M. Yuan, R. Kutney, J. E. Shively, and W. Levin (1982, Biochemistry 21, 1152-1155) the NH2-terminal sequence of the mature protein lacks the NH2-terminal Met residue. Comparison of the rat cytochrome P-450d sequence with the mouse cytochrome P3-450 cDNA sequence reported by S. Kimura, F.J. Gonzalez, and D.W. Nebert (1984, Nucl. Acids Res. 12, 2917-2928) reveals a high sequence homology with a total of 32 amino acid differences including six conferring charge changes. Prediction of the secondary structure of cytochrome P-450d yields a maximum of 17 helices, two of which may be poly(Pro)-like helices adjacent to potential membrane-spanning alpha-helices. Four of the alpha-helices are sufficiently hydrophobic to traverse the endoplasmic reticulum. The remaining helices are largely amphiphilic. Analysis of the helices in reference to predicted membrane topology suggests that cytochrome P-450d either has one large and one small globular domain separated by a transmembrane domain and anchored by NH2-terminal and COOH-terminal transmembrane domains, or has one large globular domain anchored at both ends by transmembrane domains.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
244
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
323-37
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
The primary structure of cytochrome P-450d purified from rat liver microsomes: prediction of helical regions and domain analysis.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.