title: 6-Pyruvoyltetrahydropterin synthase orthologs of either a single or dual domain structure are responsible for tetrahydrobiopterin synthesis in bacteria.
abstract: 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.
authors.affiliation: Mitochondrial Research Group, School of Biotechnology and Biomedical Science, Inje University, Kimhae 621-749, Republic of Korea.
authors.forename: Jin Sun
authors.initials: JS
authors.lastname: Kong
authors.forename: Ji-Youn
authors.initials: JY
authors.lastname: Kang
authors.forename: Hye Lim
authors.initials: HL
authors.lastname: Kim
authors.forename: O-Seob
authors.initials: OS
authors.lastname: Kwon
authors.forename: Kon Ho
authors.initials: KH
authors.lastname: Lee
authors.forename: Young Shik
authors.initials: YS
authors.lastname: Park
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D001708:Biopterins / Q000031:analogs & derivatives* / Q000096:biosynthesis; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D016296:Mutagenesis; D019761:Phosphorus-Oxygen Lyases / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D010802:Phylogeny; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D046940:Synechococcus / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D007527:Isoenzymes; D011994:Recombinant Proteins; D001708:Biopterins; D019761:Phosphorus-Oxygen Lyases; C043497:6-pyruvoyltetrahydropterin synthase; C003402:sapropterin