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

A complete structural description of the catalytic cycle of yeast pyrophosphatase.

Biochemistry - 6 Feb 2007

Oksanen Esko, Ahonen Anna-Karoliina, Tuominen Heidi, Tuominen Vesa, Lahti Reijo, Goldman Adrian, Heikinheimo Pirkko

Abstract excerpt

We have determined the structures of the wild type and seven active site variants of yeast inorganic pyrophosphatase (PPase) in the presence of Mg2+ and phosphate, providing the first complete structural description of its catalytic cycle. PPases catalyze the hydrolysis of pyrophosphate and require four divalent metal cations for catalysis; magnesium provides the highest activity. The crystal form chosen contains...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Catalysis
Share to Fungal Proteins

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

Share to Hydrogen Bonding

Share to Hydrophobic and Hydrophilic Interactions

Share to Magnesium

Share to Mutation

Share to Phosphates

Source

Identifiers

PMID: 17260952
DOI: 10.1021/bi0619977

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 · 12 closest

A complete structural description of the catalytic cycle of yeast pyrophosphatase.PMID 17260952Read ↗

The crystal structure of yeast mitochondrial type pyrophosphatase provides a model to study pathological mutations in its human ortholog.Semantic proximity Read ↗

Probing essential water in yeast pyrophosphatase by directed mutagenesis and fluoride inhibition measurements.Semantic proximity Read ↗

The structure and catalytic cycle of a sodium-pumping pyrophosphatase.Semantic proximity Read ↗

Reversible inhibition of Escherichia coli inorganic pyrophosphatase by fluoride: trapped catalytic intermediates in cryo-crystallographic studies.Semantic proximity Read ↗

Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases.Semantic proximity Read ↗

Conformational response to ligand binding in phosphomannomutase2: insights into inborn glycosylation disorder.Semantic proximity Read ↗

Conformational Dynamics of Mitochondrial Inorganic Pyrophosphatase hPPA2 and Its Changes Caused by Pathogenic MutationsSemantic proximity Read ↗

Effect of Structure Variations in the Inter-subunit Contact Zone on the Activity and Allosteric Regulation of Inorganic Pyrophosphatase from Mycobacterium tuberculosis.Semantic proximity Read ↗

Extended regulation interface coupled to the allosteric network and disease mutations in the PP2A-B56δ holoenzymeSemantic proximity Read ↗

Finding a needle in the haystack: computational modeling of Mg2+ binding in the active site of protein farnesyltransferase.Semantic proximity Read ↗

A site-directed mutagenesis study on Escherichia coli inorganic pyrophosphatase. Glutamic acid-98 and lysine-104 are important for structural integrity, whereas aspartic acids-97 and -102 are essential for catalytic activity.Semantic proximity Read ↗

Modulation of dimer stability in yeast pyrophosphatase by mutations at the subunit interface and ligand binding to the active site.Semantic proximity Read ↗

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