D-erythro-neopterin biosynthesis in the methanogenic archaea Methanococcus thermophila and Methanobacterium thermoautotrophicum deltaH.
The steps in the biosynthetic transformation of GTP to 7,8-dihydro-D-erythro-neopterin (H2neopterin), the precursor to the modified folates found in the methanogenic archaea, has been elucidated for the first time in two members of the domain Archaea. In Methanococcus thermophila and Methanobacterium thermoautotrophicum deltaH, it has been demonstrated that H2neopterin 2':3'-cyclic phosphate is an intermediate in this conversion. In addition, the formation of the pterin ring of the H2neopterin 2':3'-cyclic phosphate is catalyzed not by a single enzyme, as is known to occur with GTP cyclohydrolase I in the Eucarya and Bacteria, but rather by two or more enzymes. A 2,4,5-triamino-4(3H)-pyrimidinone-containing molecule, most likely 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate, has been identified as an intermediate in the formation of the H2neopterin 2':3'-cyclic phosphate. Synthetic H2neopterin 2':3'-cyclic phosphate was found to be readily hydrolyzed by cell extracts of M. thermophila via the H2neopterin 3'-phosphate to H2neopterin, a known precursor to the pterin portion of methanopterin.
Howell
D M
DM
Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061-0308, USA.
White
R H
RH
D001708:Biopterins / Q000031:analogs & derivatives* / Q000096:biosynthesis; D002855:Chromatography, Thin Layer; D006136:GTP Cyclohydrolase / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D017014:Methanobacterium / Q000201:enzymology / Q000378:metabolism*; D017017:Methanococcus / Q000201:enzymology / Q000378:metabolism*; D019798:Neopterin / Q000031:analogs & derivatives; D011621:Pteridines / Q000378:metabolism
C107589:7,8-dihydroneopterin 2',3'-cyclic phosphate; D011621:Pteridines; C000976:7,8-dihydroneopterin; D001708:Biopterins; D019798:Neopterin; D006160:Guanosine Triphosphate; D006136:GTP Cyclohydrolase