| pubmed-article:19317437 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:19317437 | lifeskim:mentions | umls-concept:C1335272 | lld:lifeskim |
| pubmed-article:19317437 | lifeskim:mentions | umls-concept:C2698697 | lld:lifeskim |
| pubmed-article:19317437 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:19317437 | lifeskim:mentions | umls-concept:C1418654 | lld:lifeskim |
| pubmed-article:19317437 | lifeskim:mentions | umls-concept:C0030065 | lld:lifeskim |
| pubmed-article:19317437 | lifeskim:mentions | umls-concept:C1418882 | lld:lifeskim |
| pubmed-article:19317437 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:19317437 | lifeskim:mentions | umls-concept:C0598002 | lld:lifeskim |
| pubmed-article:19317437 | lifeskim:mentions | umls-concept:C0540454 | lld:lifeskim |
| pubmed-article:19317437 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:19317437 | pubmed:dateCreated | 2009-5-12 | lld:pubmed |
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| pubmed-article:19317437 | 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. | lld:pubmed |
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| pubmed-article:19317437 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19317437 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19317437 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19317437 | pubmed:month | May | lld:pubmed |
| pubmed-article:19317437 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:19317437 | pubmed:author | pubmed-author:EalickSteven... | lld:pubmed |
| pubmed-article:19317437 | pubmed:author | pubmed-author:BegleyTadhg... | lld:pubmed |
| pubmed-article:19317437 | pubmed:author | pubmed-author:McCullochKath... | lld:pubmed |
| pubmed-article:19317437 | pubmed:author | pubmed-author:MukherjeeTath... | lld:pubmed |
| pubmed-article:19317437 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19317437 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:19317437 | pubmed:volume | 48 | lld:pubmed |
| pubmed-article:19317437 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19317437 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19317437 | pubmed:pagination | 4139-49 | lld:pubmed |
| pubmed-article:19317437 | pubmed:dateRevised | 2011-4-1 | lld:pubmed |
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