pubmed-article:16920111 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C0004611 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C1273518 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C0284927 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C1157041 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C1554184 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C1335144 | lld:lifeskim |
pubmed-article:16920111 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:16920111 | pubmed:issue | 20 | lld:pubmed |
pubmed-article:16920111 | pubmed:dateCreated | 2006-8-29 | lld:pubmed |
pubmed-article:16920111 | pubmed:abstractText | 6-Pyruvoyltetrahydropterin synthase (PTPS) catalyzes the second step of tetrahydrobiopterin (BH4) synthesis. We previously identified PTPS orthologs (bPTPS-Is) in bacteria which do not produce BH4. In this study we disrupted the gene encoding bPTPS-I in Synechococcus sp. PCC 7942, which produces BH4-glucoside. The mutant was normal in BH4-glucoside production, demonstrating that bPTPS-I does not participate in BH4 synthesis in vivo and bringing us a new PTPS ortholog (bPTPS-II) of a bimodular polypeptide. The recombinant Synechococcus bPTPS-II was assayed in vitro to show PTPS activity higher than human enzyme. Further computational analysis revealed the presence of mono and bimodular bPTPS-II orthologs mostly in green sulfur bacteria and cyanobacteria, respectively, which are well known for BH4-glycoside production. In summary we found new bacterial PTPS orthologs, having either a single or dual domain structure and being responsible for BH4 synthesis in vivo, thereby disclosing all the bacterial PTPS homologs. | lld:pubmed |
pubmed-article:16920111 | pubmed:language | eng | lld:pubmed |
pubmed-article:16920111 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16920111 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16920111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16920111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16920111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16920111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16920111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16920111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16920111 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16920111 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16920111 | pubmed:month | Sep | lld:pubmed |
pubmed-article:16920111 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:16920111 | pubmed:author | pubmed-author:ParkYoung... | lld:pubmed |
pubmed-article:16920111 | pubmed:author | pubmed-author:LeeKon HoKH | lld:pubmed |
pubmed-article:16920111 | pubmed:author | pubmed-author:KongJin SunJS | lld:pubmed |
pubmed-article:16920111 | pubmed:author | pubmed-author:KangJi-YounJY | lld:pubmed |
pubmed-article:16920111 | pubmed:author | pubmed-author:KimHye LimHL | lld:pubmed |
pubmed-article:16920111 | pubmed:author | pubmed-author:KwonO-SeobOS | lld:pubmed |
pubmed-article:16920111 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16920111 | pubmed:day | 4 | lld:pubmed |
pubmed-article:16920111 | pubmed:volume | 580 | lld:pubmed |
pubmed-article:16920111 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16920111 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16920111 | pubmed:pagination | 4900-4 | lld:pubmed |
pubmed-article:16920111 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:16920111 | pubmed:meshHeading | pubmed-meshheading:16920111... | lld:pubmed |
pubmed-article:16920111 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16920111 | pubmed:articleTitle | 6-Pyruvoyltetrahydropterin synthase orthologs of either a single or dual domain structure are responsible for tetrahydrobiopterin synthesis in bacteria. | lld:pubmed |
pubmed-article:16920111 | pubmed:affiliation | Mitochondrial Research Group, School of Biotechnology and Biomedical Science, Inje University, Kimhae 621-749, Republic of Korea. | lld:pubmed |
pubmed-article:16920111 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16920111 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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