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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1991-6-6
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pubmed:abstractText |
The role of conserved arginine residues in hydroxymethylbilane synthase was investigated by replacing these residues in the enzyme from Escherichia coli with leucine residues by using site-directed mutagenesis. The kinetic parameters for these mutant enzymes and studies on the formation of intermediate enzyme-substrate complexes indicate that several of these arginine residues are involved in binding the carboxylate side chains of the pyrromethane cofactor and the growing oligopyrrole chain.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-190679,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-2477247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-2510713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-2664584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-2875434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3040684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3054815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3069132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3079571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3325863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3368319,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3421931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3422427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3529035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3548707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3895052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-3913886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2025226-6769048
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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 |
Apr
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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 |
275 ( Pt 2)
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pubmed:geneSymbol |
hemC
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
447-52
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2025226-Amino Acid Sequence,
pubmed-meshheading:2025226-Arginine,
pubmed-meshheading:2025226-Binding Sites,
pubmed-meshheading:2025226-Escherichia coli,
pubmed-meshheading:2025226-Genes, Bacterial,
pubmed-meshheading:2025226-Hydroxymethylbilane Synthase,
pubmed-meshheading:2025226-Kinetics,
pubmed-meshheading:2025226-Molecular Sequence Data,
pubmed-meshheading:2025226-Mutagenesis, Site-Directed,
pubmed-meshheading:2025226-Plasmids,
pubmed-meshheading:2025226-Recombinant Proteins,
pubmed-meshheading:2025226-Sequence Homology, Nucleic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding.
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pubmed:affiliation |
University Chemical Laboratory, University of Cambridge, U.K.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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