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pubmed-article:16920111pubmed:abstractText6-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
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pubmed-article:16920111pubmed:authorpubmed-author:ParkYoung...lld:pubmed
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pubmed-article:16920111pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:16920111pubmed:articleTitle6-Pyruvoyltetrahydropterin synthase orthologs of either a single or dual domain structure are responsible for tetrahydrobiopterin synthesis in bacteria.lld:pubmed
pubmed-article:16920111pubmed:affiliationMitochondrial Research Group, School of Biotechnology and Biomedical Science, Inje University, Kimhae 621-749, Republic of Korea.lld:pubmed
pubmed-article:16920111pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16920111pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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