Identification of d-erythro-Dihydroneopterin Triphosphate, the First Product of Pteridine Biosynthesis in Comamonas Sp. (ATCC 11299a)

Plowman, Jacqueline; Cone, Joyce E.; Guroff, Gordon

doi:10.1016/s0021-9258(20)79764-4

Cited by 17 publications

(1 citation statement)

References 17 publications

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“…It has been demonstrated that neopterin 3‘-triphosphate can be chemically converted into neopterin 2‘,3‘-cyclic phosphate when exposed to basic work-up conditions or certain chromatographic conditions ( , ). Such a transformation could explain our detection of neopterin 2‘,3‘-cyclic phosphate.…”

Section: Resultsmentioning

confidence: 99%

Characterization of an Fe²⁺-Dependent Archaeal-Specific GTP Cyclohydrolase, MptA, from Methanocaldococcus jannaschii

Grochowski

Leung

et al. 2007

Biochemistry

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The first step in the biosynthesis of pterins in bacteria and plants is the conversion of GTP to 7,8-dihydro-d-neopterin triphosphate catalyzed by GTP cyclohydrolase I (GTPCHI). Although GTP has been shown to be a precursor of pterins in archaea, homologues of GTPCHI have not been identified in most archaeal genomes. Here we report the identification of a new GTP cyclohydrolase that converts GTP to 7,8-dihydro-d-neopterin 2',3'-cyclic phosphate, the first intermediate in methanopterin biosynthesis in methanogenic archaea. The enzyme from Methanocaldococcus jannaschii is designated MptA to indicate that it catalyzes the first step in the biosynthesis of methanopterin. MptA is the archetype of a new class of GTP cyclohydrolases that catalyzes a series of reactions most similar to that seen with GTPCHI but unique in that the cyclic phosphate is the product. MptA was found to require Fe2+ for activity. Mutation of conserved histidine residues H200N, H293N, and H295N, expected to be involved in Fe2+ binding, resulted in reduced enzymatic activity but no reduction in the amount of bound iron.

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Section: Resultsmentioning

confidence: 99%

Characterization of an Fe²⁺-Dependent Archaeal-Specific GTP Cyclohydrolase, MptA, from Methanocaldococcus jannaschii

Grochowski

Leung

et al. 2007

Biochemistry

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The nature of the multiple forms of triphosphate synthetase

Jackson

Shiota

1975

Biochimica et Biophysica Acta (BBA) - Enzymology

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Polarization fluoroimmunoassay of biopterin and neopterin in human urine

Sawada

Yamaguchi

Sugimoto

et al. 1984

Clinica Chimica Acta

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Identification of d-erythro-Dihydroneopterin Triphosphate, the First Product of Pteridine Biosynthesis in Comamonas Sp. (ATCC 11299a)

Cited by 17 publications

References 17 publications

Characterization of an Fe²⁺-Dependent Archaeal-Specific GTP Cyclohydrolase, MptA, from Methanocaldococcus jannaschii

Characterization of an Fe²⁺-Dependent Archaeal-Specific GTP Cyclohydrolase, MptA, from Methanocaldococcus jannaschii

The nature of the multiple forms of triphosphate synthetase

Polarization fluoroimmunoassay of biopterin and neopterin in human urine

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Identification of d-erythro-Dihydroneopterin Triphosphate, the First Product of Pteridine Biosynthesis in Comamonas Sp. (ATCC 11299a)

Cited by 17 publications

References 17 publications

Characterization of an Fe2+-Dependent Archaeal-Specific GTP Cyclohydrolase, MptA, from Methanocaldococcus jannaschii

Characterization of an Fe2+-Dependent Archaeal-Specific GTP Cyclohydrolase, MptA, from Methanocaldococcus jannaschii

The nature of the multiple forms of triphosphate synthetase

Polarization fluoroimmunoassay of biopterin and neopterin in human urine

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Characterization of an Fe²⁺-Dependent Archaeal-Specific GTP Cyclohydrolase, MptA, from Methanocaldococcus jannaschii

Characterization of an Fe²⁺-Dependent Archaeal-Specific GTP Cyclohydrolase, MptA, from Methanocaldococcus jannaschii