rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2000-1-27
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pubmed:databankReference |
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pubmed:abstractText |
The epoxide hydrolase (EH)-encoding gene (EPH1) from the basidiomycetous yeast Xanthophyllomyces dendrorhous was isolated. The genomic sequence has a 1,236-bp open reading frame which is interrupted by eight introns that encode a 411-amino-acid polypeptide with a calculated molecular mass of 46.2 kDa. The amino acid sequence is similar to that of microsomal EH and belongs to the alpha/beta hydrolase fold family. The EPH1 gene was not essential for growth of X. dendrorhous in rich medium under laboratory conditions. The Eph1-encoding cDNA was functionally expressed in Escherichia coli. A sixfold increase in specific activity was observed when we used resting cells rather than X. dendrorhous. The epoxides 1,2-epoxyhexane and 1-methylcyclohexene oxide were substrates for both native and recombinant Eph1. Isolation and characterization of the X. dendrorhous EH-encoding gene are essential steps in developing a yeast EH-based epoxide biotransformation system.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-10207888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-1409539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-2729997,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-2821541,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-2891713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-3755318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-4584115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-6280875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-6418203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-6800789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-6967314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-7001447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-7204381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-7732720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-7920715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-7920716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-7980469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-8199297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-8307189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-8645304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-9151984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-9169427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-9364747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-9578475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-9748436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10584004-9854022
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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 |
Dec
|
pubmed:issn |
0099-2240
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5459-63
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10584004-Amino Acid Sequence,
pubmed-meshheading:10584004-Animals,
pubmed-meshheading:10584004-Basidiomycota,
pubmed-meshheading:10584004-Cloning, Molecular,
pubmed-meshheading:10584004-Epoxide Hydrolases,
pubmed-meshheading:10584004-Escherichia coli,
pubmed-meshheading:10584004-Genes, Fungal,
pubmed-meshheading:10584004-Microsomes,
pubmed-meshheading:10584004-Molecular Sequence Data,
pubmed-meshheading:10584004-Molecular Weight,
pubmed-meshheading:10584004-Open Reading Frames,
pubmed-meshheading:10584004-Polymerase Chain Reaction,
pubmed-meshheading:10584004-Protein Folding,
pubmed-meshheading:10584004-Rabbits,
pubmed-meshheading:10584004-Rats,
pubmed-meshheading:10584004-Recombinant Proteins,
pubmed-meshheading:10584004-Restriction Mapping,
pubmed-meshheading:10584004-Sequence Alignment,
pubmed-meshheading:10584004-Sequence Homology, Amino Acid
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pubmed:year |
1999
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pubmed:articleTitle |
Isolation and characterization of the epoxide hydrolase-encoding gene from Xanthophyllomyces dendrorhous.
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pubmed:affiliation |
Division of Industrial Microbiology, Department of Food Technology and Nutritional Sciences, Wageningen Agricultural University, 6700 EV Wageningen, The Netherlands. hans.visser@imb.ftns.wau.nl
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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