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rdf:type |
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lifeskim:mentions |
umls-concept:C0004755,
umls-concept:C0014834,
umls-concept:C0017262,
umls-concept:C0017837,
umls-concept:C0030016,
umls-concept:C0035720,
umls-concept:C0162768,
umls-concept:C0185117,
umls-concept:C0205177,
umls-concept:C1095831,
umls-concept:C2911684
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pubmed:issue |
17
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pubmed:dateCreated |
1996-10-31
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pubmed:abstractText |
delta-Aminolevulinate in plants, algae, cyanobacteria, and several other bacteria such as Escherichia coli and Bacillus subtilis is synthesized from glutamate by means of a tRNA(Glu) mediated pathway. The enzyme glutamyl tRNA(Glu) reductase catalyzes the second step in this pathway, the reduction of tRNA bound glutamate to give glutamate 1-semialdehyde. The hemA gene from barley encoding the glutamyl tRNA(Glu) reductase was expressed in E. coli cells joined at its amino terminal end to Schistosoma japonicum glutathione S-transferase (GST). GST-glutamyl tRNA(Glu) reductase fusion protein and the reductase released from it by thrombin digestion catalyzed the reduction of glutamyl tRNA(Glu) to glutamate 1-semialdehyde. The specific activity of the fusion protein was 120 pmol.micrograms-1.min-1. The fusion protein used tRNA(Glu) from barley chloroplasts preferentially to E. coli tRNA(Glu) and its activity was inhibited by hemin. It migrated as an 82-kDa polypeptide with SDS/PAGE and eluted with an apparent molecular mass of 450 kDa from Superose 12. After removal of the GST by thrombin, the protein migrated as an approximately equal to 60-kDa polypeptide with SDS/PAGE, whereas gel filtration on Superose 12 yielded an apparent molecule mass of 250 kDa. Isolated fusion protein contained heme, which could be reduced by NADPH and oxidized by air.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-1459859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-1536660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-1569081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-1793335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-1903397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-1990004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-2110138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-2303495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-2407729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-2449095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-2466658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-2544564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-2548996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-2651407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-2656630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-2664455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-3454661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-7548209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-7665501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-7764570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-7908550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8799193-7957167
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Aminolevulinic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamates,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Hemin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glutamate-1-semialdehyde,
http://linkedlifedata.com/resource/pubmed/chemical/glutamyl tRNA reductase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
93
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9287-91
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:8799193-Aldehyde Oxidoreductases,
pubmed-meshheading:8799193-Amino Acid Sequence,
pubmed-meshheading:8799193-Aminolevulinic Acid,
pubmed-meshheading:8799193-Base Sequence,
pubmed-meshheading:8799193-Cytochromes,
pubmed-meshheading:8799193-Escherichia coli,
pubmed-meshheading:8799193-Glutamates,
pubmed-meshheading:8799193-Glutamic Acid,
pubmed-meshheading:8799193-Glutathione Transferase,
pubmed-meshheading:8799193-Heme,
pubmed-meshheading:8799193-Hemin,
pubmed-meshheading:8799193-Hordeum,
pubmed-meshheading:8799193-Molecular Sequence Data,
pubmed-meshheading:8799193-Oxidation-Reduction,
pubmed-meshheading:8799193-Recombinant Fusion Proteins,
pubmed-meshheading:8799193-Spectrophotometry
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pubmed:year |
1996
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pubmed:articleTitle |
Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase.
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pubmed:affiliation |
Carlsberg Laboratory, Department of Physiology, Copenhagen-Valby, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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