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rdf:type |
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lifeskim:mentions |
umls-concept:C0010762,
umls-concept:C0014239,
umls-concept:C0017262,
umls-concept:C0036025,
umls-concept:C0038592,
umls-concept:C0185117,
umls-concept:C0205225,
umls-concept:C0678594,
umls-concept:C0997659,
umls-concept:C1280500,
umls-concept:C1514485,
umls-concept:C1707455,
umls-concept:C2911684
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pubmed:issue |
2
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pubmed:dateCreated |
1991-12-10
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pubmed:databankReference |
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pubmed:abstractText |
cDNAs were cloned, sequenced and expressed which encode two different cytochrome P-450 forms of the alkane-assimilating yeast Candida maltosa, designated as P-450Cm1 and P-450Cm2. The amino acid sequences deduced were about 55% identical. Expression in Saccharomyces cerevisiae resulted in the formation of intact microsomal P-450 systems catalyzing the hydroxylation of n-hexadecane and lauric acid with significantly different substrate preferences. A massive proliferation of the endoplasmic reticulum was observed in the S. cerevisiae cells which produced P-450. Depending on the P-450 form expressed, distinctly organized stacks of paired membranes appeared and occupied considerable areas of the cytoplasm. As shown by immunoelectron microscopy for P-450Cm1, the protein expressed was highly concentrated within these newly formed membrane structures.
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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 |
Aug
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pubmed:issn |
0171-9335
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
55
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
336-45
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1935996-Amino Acid Sequence,
pubmed-meshheading:1935996-Base Sequence,
pubmed-meshheading:1935996-Blotting, Western,
pubmed-meshheading:1935996-Candida,
pubmed-meshheading:1935996-Cloning, Molecular,
pubmed-meshheading:1935996-Cytochrome P-450 Enzyme System,
pubmed-meshheading:1935996-DNA,
pubmed-meshheading:1935996-Endoplasmic Reticulum,
pubmed-meshheading:1935996-Gene Expression,
pubmed-meshheading:1935996-Genes, Fungal,
pubmed-meshheading:1935996-Hydroxylation,
pubmed-meshheading:1935996-Immunohistochemistry,
pubmed-meshheading:1935996-Isoenzymes,
pubmed-meshheading:1935996-Microscopy, Electron,
pubmed-meshheading:1935996-Microsomes,
pubmed-meshheading:1935996-Molecular Sequence Data,
pubmed-meshheading:1935996-Multigene Family,
pubmed-meshheading:1935996-Saccharomyces cerevisiae,
pubmed-meshheading:1935996-Sequence Alignment,
pubmed-meshheading:1935996-Substrate Specificity
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pubmed:year |
1991
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pubmed:articleTitle |
Comparison of two cytochromes P-450 from Candida maltosa: primary structures, substrate specificities and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum.
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pubmed:affiliation |
Central Institute of Molecular Biology, Berlin-Buch/Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study
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