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6‐Pyruvoyltetrahydropterin synthase orthologs of either a single or dual domain structure are responsible for tetrahydrobiopterin synthesis in bacteria
Author(s) -
Kong Jin Sun,
Kang Ji-Youn,
Kim Hye Lim,
Kwon O-Seob,
Lee Kon Ho,
Park Young Shik
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.08.006
Subject(s) - tetrahydrobiopterin , bacteria , biochemistry , enzyme , atp synthase , mutant , gene , chemistry , biosynthesis , biology , cofactor , genetics
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.