Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase.

Journal of molecular biology - 26 Feb 1999

Ploom T, Thöny B, Yim J, Lee S, Nar H, Leimbacher W, Richardson J, Huber R, Auerbach G

Abstract excerpt

The enzyme 6-pyruvoyl tetrahydropterin synthase (PTPS) catalyses the second step in the de novo biosynthesis of tetrahydrobiopterin, the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin. The Zn and Mg-dependent reaction includes a triphosphate elimination, a stereospecific reduction of the N5-C6 double bond and the oxidation of both side-chain hydroxyl groups. The crystal structure of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biopterins
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Kinetics

Share to Molecular Structure

Share to Phosphorus-Oxygen Lyases

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 10024455
DOI: 10.1006/jmbi.1998.2511

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 10 closest

Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase.PMID 10024455Read ↗

Structural basis of autoregulation of phenylalanine hydroxylase.Semantic proximity Read ↗

The structure of full-length human phenylalanine hydroxylase in complex with tetrahydrobiopterinSemantic proximity Read ↗

Structural and functional consequences of mutations in 6-pyruvoyltetrahydropterin synthase causing hyperphenylalaninemia in humans. Phosphorylation is a requirement for in vivo activity.Semantic proximity Read ↗

High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin.Semantic proximity Read ↗

The structure of Plasmodium falciparum hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase reveals the basis of sulfa resistance.Semantic proximity Read ↗

Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments.Semantic proximity Read ↗

Serine 19 of human 6-pyruvoyltetrahydropterin synthase is phosphorylated by cGMP protein kinase II.Semantic proximity Read ↗

Catalytic mechanism of SGAP, a double-zinc aminopeptidase from Streptomyces griseus.Semantic proximity Read ↗

An additional substrate binding site in a bacterial phenylalanine hydroxylase.Semantic proximity Read ↗

Crystal structure of the beta Ser178--> Pro mutant of tryptophan synthase. A "knock-out" allosteric enzyme.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.