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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1997-10-16
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pubmed:databankReference |
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pubmed:abstractText |
cDNA species coding for alpha-methylacyl-CoA racemase were cloned from rat and mouse liver cDNA libraries and characterized. The rat liver lambdagt11 cDNA expression library was screened with anti-racemase IgG [Schmitz, Albers, Fingerhut and Conzelmann (1995) Eur. J. Biochem.231, 815-822]. Several full-length clones were obtained that contained an open reading frame of 1083 bp, coding for a protein of 361 amino acid residues with a predicted molecular mass of 39679 Da. The sequences of three peptides that were isolated by HPLC from a tryptic digest of purified rat liver racemase fully matched the cDNA-derived amino acid sequence. The cDNA coding for mouse racemase was cloned from a mouse liver lambdaZAP cDNA expression library and sequenced. The coding region of 1080 bp codes for a 360-residue protein (molecular mass 39558 Da) that shares 89.7% similarity with the rat protein. Expression of the rat racemase as are combinant protein in Escherichia coli with the pTrcHisB-expression vector yielded enzymically active protein. The amino acid sequences of alpha-methylacyl-CoA racemases do not resemble any known sequence of beta-oxidation or auxiliary enzymes, supporting the view of a highly diverse evolutionary origin of enzymes acting on fatty acyl-CoA S-esters.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-1417723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-17805694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-2231712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-2452737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-28327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-3015598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-5838653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-5970517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-6209040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-7461136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-7541878,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-7649182,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-8020470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-8654595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-8694830,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-8769411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-8994879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-9106621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-9119009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9307041-942051
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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 |
Sep
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
326 ( Pt 3)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
883-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9307041-Amino Acid Sequence,
pubmed-meshheading:9307041-Animals,
pubmed-meshheading:9307041-Base Sequence,
pubmed-meshheading:9307041-Cloning, Molecular,
pubmed-meshheading:9307041-DNA, Complementary,
pubmed-meshheading:9307041-Escherichia coli,
pubmed-meshheading:9307041-Liver,
pubmed-meshheading:9307041-Mice,
pubmed-meshheading:9307041-Molecular Sequence Data,
pubmed-meshheading:9307041-Racemases and Epimerases,
pubmed-meshheading:9307041-Rats,
pubmed-meshheading:9307041-Recombinant Proteins,
pubmed-meshheading:9307041-Sequence Alignment
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pubmed:year |
1997
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pubmed:articleTitle |
Molecular cloning of cDNA species for rat and mouse liver alpha-methylacyl-CoA racemases.
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pubmed:affiliation |
Theodor-Boveri-Institut für Biowissenschaften (Biozentrum) der Universität Würzburg, Am Hubland, D-97074 Würzburg, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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