Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2009-5-12
pubmed:databankReference
pubmed:abstractText
A vitamin B(6) degradative pathway has recently been identified and characterized in Mesorhizobium loti MAFF303099. One of the enzymes on this pathway, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO), is a flavin-dependent enzyme and catalyzes the oxidative ring-opening of 2-methyl-3-hydroxypyridine-5-carboxylic acid to form E-2-(acetamino-methylene)succinate. The gene for this enzyme has been cloned, and the corresponding protein has been overexpressed in Escherichia coli and purified. The crystal structure of MHPCO has been solved to 2.1 A using SAD phasing with and without the substrate MHPC bound. These crystal structures provide insight into the reaction mechanism and suggest roles for active site residues in the catalysis of a novel oxidative ring-opening reaction.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-11214968, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-11805318, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-12192063, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-12499537, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-13610871, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-13610872, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-15049701, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-15572765, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-16226926, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-16274228, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-16712999, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-16730633, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-17045293, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-17270714, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-17275397, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-17868768, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-17873060, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-17973403, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-18216065, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-18416536, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-18440023, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-18476725, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-18635903, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-40036, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-4306031, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-5700707, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-7217080, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-7217081, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-7737455, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-8804824, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-9054568, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-9201954, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-9207074, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-9254694, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-9374863, http://linkedlifedata.com/resource/pubmed/commentcorrection/19317437-9757107
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
19
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4139-49
pubmed:dateRevised
2011-4-1
pubmed:meshHeading
pubmed-meshheading:19317437-Histidine, pubmed-meshheading:19317437-Oxidation-Reduction, pubmed-meshheading:19317437-Catalysis, pubmed-meshheading:19317437-Nicotinic Acids, pubmed-meshheading:19317437-Escherichia coli, pubmed-meshheading:19317437-Crystallography, X-Ray, pubmed-meshheading:19317437-Ultracentrifugation, pubmed-meshheading:19317437-Flavin-Adenine Dinucleotide, pubmed-meshheading:19317437-Models, Molecular, pubmed-meshheading:19317437-Mixed Function Oxygenases, pubmed-meshheading:19317437-Protein Binding, pubmed-meshheading:19317437-Binding Sites, pubmed-meshheading:19317437-Substrate Specificity, pubmed-meshheading:19317437-Dimerization, pubmed-meshheading:19317437-Hydrogen Bonding, pubmed-meshheading:19317437-Protein Structure, Secondary, pubmed-meshheading:19317437-Cloning, Molecular, pubmed-meshheading:19317437-Ligands, pubmed-meshheading:19317437-Alphaproteobacteria, pubmed-meshheading:19317437-Recombinant Proteins
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