The C-6 proton of tetrahydrobiopterin is acquired from water, not NADPH, during de novo biosynthesis.

Smith, Gary K.; Cichetti, J A; Chandrasurin, Pisal; Nichol, Charles A.

doi:10.1016/s0021-9258(18)89006-8

Cited by 12 publications

(1 citation statement)

References 13 publications

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“…However, such acidic conditions cannot be used in our assay, because it will result in acidcatalyzed opening of the five-membered cyclic phosphate. Iodine oxidation in basic solution, which will prevent this hydrolysis of the cyclic phosphate, can also do the desired oxidation (19); however, basic solution cannot be used in our assay because it is known to result in removal of the chain from the pterin ring during oxidation (19). In this work we used I 2 in methanol at neutral pH to oxidize the dihydroneopterins to pterins.…”

Section: Identification Of Mptbmentioning

confidence: 99%

An Fe²⁺-Dependent Cyclic Phosphodiesterase Catalyzes the Hydrolysis of 7,8-Dihydro-d-neopterin 2′,3′-Cyclic Phosphate in Methanopterin Biosynthesis

Mashhadi

White

2009

Biochemistry

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7,8-Dihydro-D-neopterin 2',3'-cyclic phosphate (H(2)N-cP) is the first intermediate in biosynthesis of the pterin portion of tetrahydromethanopterin (H(4)MPT), a C(1) carrier coenzyme first identified in the methanogenic archaea. This intermediate is produced from GTP by MptA (MJ0775 gene product), a new class of GTP cyclohydrolase I [Grochowski, L. L., Xu, H., Leung, K., and White, R. H. (2007) Biochemistry 46, 6658-6667]. Here we report the identification of a cyclic phosphodiesterase that hydrolyzes the cyclic phosphate of H(2)N-cP and converts it to a mixture of 7,8-dihydro-D-neopterin 2'-monophosphate and 7,8-dihydro-d-neopterin 3'-monophosphate. The enzyme from Methanocaldococcus jannachii is designated MptB (MJ0837 gene product) to indicate that it catalyzes the second step of the biosynthesis of methanopterin. MptB is a member of the HD domain superfamily of enzymes, which require divalent metals for activity. Direct metal analysis of the recombinant enzyme demonstrated that MptB contained 1.0 mol of zinc and 0.8 mol of iron per protomer. MptB requires Fe(2+) for activity, the same as observed for MptA. Thus the first two enzymes involved in H(4)MPT biosynthesis in the archaea are Fe(2+) dependent.

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Section: Identification Of Mptbmentioning

confidence: 99%

An Fe²⁺-Dependent Cyclic Phosphodiesterase Catalyzes the Hydrolysis of 7,8-Dihydro-d-neopterin 2′,3′-Cyclic Phosphate in Methanopterin Biosynthesis

Mashhadi

White

2009

Biochemistry

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On the role of sepiapterin reductase in the biosynthesis of tetrahydrobiopterin

Smith¹

1987

Archives of Biochemistry and Biophysics

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Biosynthesis of biopterin studies on the mechanism of 6-pyruvoyltetrahydropteridine synthase

Van

Katzenmeier

Schwarzkopf

et al. 1988

Biochemical and Biophysical Research Communications

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The C-6 proton of tetrahydrobiopterin is acquired from water, not NADPH, during de novo biosynthesis.

Cited by 12 publications

References 13 publications

An Fe²⁺-Dependent Cyclic Phosphodiesterase Catalyzes the Hydrolysis of 7,8-Dihydro-d-neopterin 2′,3′-Cyclic Phosphate in Methanopterin Biosynthesis

An Fe²⁺-Dependent Cyclic Phosphodiesterase Catalyzes the Hydrolysis of 7,8-Dihydro-d-neopterin 2′,3′-Cyclic Phosphate in Methanopterin Biosynthesis

On the role of sepiapterin reductase in the biosynthesis of tetrahydrobiopterin

Biosynthesis of biopterin studies on the mechanism of 6-pyruvoyltetrahydropteridine synthase

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The C-6 proton of tetrahydrobiopterin is acquired from water, not NADPH, during de novo biosynthesis.

Cited by 12 publications

References 13 publications

An Fe2+-Dependent Cyclic Phosphodiesterase Catalyzes the Hydrolysis of 7,8-Dihydro-d-neopterin 2′,3′-Cyclic Phosphate in Methanopterin Biosynthesis

An Fe2+-Dependent Cyclic Phosphodiesterase Catalyzes the Hydrolysis of 7,8-Dihydro-d-neopterin 2′,3′-Cyclic Phosphate in Methanopterin Biosynthesis

On the role of sepiapterin reductase in the biosynthesis of tetrahydrobiopterin

Biosynthesis of biopterin studies on the mechanism of 6-pyruvoyltetrahydropteridine synthase

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Product

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An Fe²⁺-Dependent Cyclic Phosphodiesterase Catalyzes the Hydrolysis of 7,8-Dihydro-d-neopterin 2′,3′-Cyclic Phosphate in Methanopterin Biosynthesis

An Fe²⁺-Dependent Cyclic Phosphodiesterase Catalyzes the Hydrolysis of 7,8-Dihydro-d-neopterin 2′,3′-Cyclic Phosphate in Methanopterin Biosynthesis